Abstract
The endoplasmic reticulum (ER) is the port of entry of proteins into the endomembrane system, and it is also involved in lipid biosynthesis and storage. This organelle contains a number of soluble and membrane-associated enzymes and molecular chaperones, which assist the folding and maturation of proteins and the deposition of lipid storage compounds. The regulation of translocation of proteins into the ER and their subsequent maturation within the organelle have been studied in detail in mammalian and yeast cells, and more recently also in plants. These studies showed that in general the functions of the ER in protein synthesis and maturation have been highly conserved between the different organisms. Yet, the ER of plants possesses some additional functions not found in mammalian and yeast cells. This compartment is involved in cell to cell communication via the plasmodesmata, and, in specialized cells, it serves as a storage site for proteins. The plant ER is also equipped with enzymes and structural proteins which are involved in the process of oil body biogenesis and lipid storage. In this review we discuss the components of the plant ER and their function in protein maturation and biogenesis of oil bodies. Due to the large number of cited papers, we were not able to cite all individual references and in many cases we refer the readers to reviews and references therein. We apologize to the authors whose references are not cited.
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References
Abeijon C, Hirschberg CB: Topography of glycosylation reactions in the endoplasmic reticulum. Trends Biochem Sci 17:32–36 (1992).
Abell BM, Holbrook LA, Abenes M, Murphy DJ, Hills MJ, Moloney MM: Role of the proline knot motif in oleosin endoplasmic reticulum topology and oil body targeting. Plant Cell 9: 1481–1493 (1997).
Allen S, Nairn HY, Bulleid NJ: Intracellular folding of tissue-type plasminogen activator. Effects of disulfide bond formation on N-linked glycosylation and secretion. J Biol Chem 270:4797–4804 (1995).
Altschuler Y, Galili G: Role of conserved cysteines of a wheat gliadin in its transport and assembly into protein bodies in Xenopus oocytes. J Biol Chem 269: 6677–6682 (1994).
Altschuler Y, Rosenberg R, Harel R, Galili G: The N-and C-terminal regions regulate the transport of wheat γ-gliadin through the endoplasmic reticulum in Xenopus oocytes. Plant Cell 5: 443–450 (1993).
Andrews DW, Johnson AE: The translocon: more than a hole in the ER membrane? Trends Biochem Sci 21: 365–368 (1996).
Anfinsen CB: Principles that govern the folding of protein chains. Science 181: 223–230 (1973).
Argos P, Pederson K, Marks MD, Larkins BA: A structural model for maize zein proteins. J Biol Chem 257: 9984–9990 (1994).
Aridor M, Weissman J, Bannykh S, Nuoffer C, Balch WE: Cargo selection by the COPII budding machinery during export from the ER. J Cell Biol 141: 61–70 (1998).
Bagga S, Adams H, Kemp JD, C: S-G: Accumulation of the 15-kD zein in novel protein bodies in transgenic tobacco. Plant Physiol 107: 13–23. (1995).
Bagga S, Adams HP, Rodriguez FD, Kemp JD, Sengupta-Gopalan C: Coexpression of the maize δ-zein and β-zein genes results in stable accumulation of δ-zein in endoplasmic reticulum-derived protein bodies formed by β-zein. Plant Cell 9: 1683–1696 (1997).
Balch W, McCaffery JM, Plutner H, Farquhar MC: Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum. Cell 76: 841–852 (1994).
Barlowe C, Orci L, Yeung T, Hosobuchi M, Hamamoto S, Salama N, Rexach MF, Ravazzola M, Amherdt M, Scheckman R: COPII: a membrane coat formed by sec proteins thet drive vesicle budding from the endolasmic reticulum. Cell 77:895–907 (1994).
Bause E: Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes. Biochem J 209: 331–336 (1983).
Bird P, Gething M-J, Sambrook J: Translocation in yeast and mammlian cells: not all signal sequences are functionally equivalent. J Cell Biol 105: 2905–2914 (1987).
Bollini R, Chrispeels MJ: The rough endoplasmic reticulum is the site of reserve-protein synthesis in developing Phaseolus vulgaris cotyledons. Planta 146: 487–501 (1979).
Bollini R, Vitale A, Chrispeels MJ: In vivo and in vitro processing of seed reserve protein in the endoplasmic reticulum: evidence for two glycosylation steps. J Cell Biol 96: 999–1007 (1983).
orgese N, D’Arrigo A, De Silvestris M, Pietrini G: NADH-cytochrome b5 reductase and cytochrome b5. The problem of posttranslational targeting to the endoplasmic reticulum. In: Borgese N, Harris JR (eds) Subcellular Biochemistry, Endoplasmic Reticulum, pp. 313–341. Plenum Press, New York (1993).
Boston RS, Fontes EBP, Shank BB, Wrobel RL: Increased expression of the maize immunoglobulin binding protein homolog b-70 in three zein regulatory mutants. Plant Cell 3: 497–505 (1991).
Boston RS, Gillikin JW, Wrobel RL: Coordinate induction of three ER-Iumenal stress proteins in maize endosperm mutants. J Cell Biochem 19A: 143 (1996).
Boston RS, Viitanen PV, Vierling E: Molecular chaperones and protein folding in plants. Plant Mol Biol 34: 191–222 (1996).
Breiman A, Fawcett TW, Ghirardi ML, Mattoo AK: Plant organelles contain distinct peptidylprolyl cis, trans-isomerases. J Biol Chem 267: 21293–21296 (1992).
Brodsky JL, McCracken AA: ER-associated and proteasome-mediated protein degradation: how two topologicals restricted events come together. Trends Cell Biol 7:151–156 (1997).
Bulleid NJ, Freedman RB: Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes. Nature 335: 649–651 (1988).
Campos N, Boronat A: Targeting and topology in the membrane of plant 3-hydroxy-3-methylglutaryl coenzyme A reductase. Plant Cell 7: 2163–2174 (1995).
Campos N, Palau J, Torrent M, Ludevid D: Signal recognition-like particles are present in maize. J Biol Chem 263:9646–9650 (1988).
Campos N, Palau J, Zwieb C: Diversity of 7 SL RNA from the signal recognition particle of maize endosperm. Nucl Acids Res 17: 1573–1588 (1989).
Ceriotti A, Colman A: Binding to membrane within the ER cannot explain the retention of the glucose-regulated protein GRP78 in Xenopus oocytes. EMBO J 7: 633–638 (1988).
Ceriotti A, Pedrazzini E, Fabbrini MS, Zoppè M, Bollini R, Vitale A: Expression of wild-type and mutated vacuolar storage protein phaseolin in Xenopus oocytes reveals relationships between assembly and intracellular transport. Eur Biochem 202: 959-968 (1991).
Chen F, Hayes PM, Mulrooney DM, Pan A: Identification and characterization of CDNA clones encoding plant calreticulin. Plant Cell 6: 83@-843 (1994).
Chirico Wj, Waters MG, Blobel G: 70K heat shock related proteins stimulate protein translocation into microsomes. Nature 332: 805–810 (1988).
Chittenden K, Gowda K, Black SD, Zwieb C: Interaction of rice and human SRP19 polypeptides with signal recognition particle RNA. Plant Mol Biol 34: 507–515 (1997).
Chrispeels MJ: Sorting of proteins in the secretory system. Annu Rev Plant Physiol Plant Mol Biol 42: 21–53 (1991).
Coleman CE, Hewrman EH, Takasaki K, Larkins BA: The maizey γ-zein sequesters α-zein and stabilizes its accumulation in protein bodies of transgenic tobacco endosperm. Plant Cell 8: 2335–2345 (1996).
Coleman CE, Lopes MA, Gillikin IW, Boston RS, Larkius BA: A defective signal peptide in the maize high-lysine mutant fluory-2. Proc Natl Acad Sci USA 92: 6828–6831 (1995).
Cooper JB, Heuser JE, Varner JE: 3,4-dehydroproline inhibits cell wall assembly and cell division in tobacco protoplasts. Plant Physiol 104: 747–752 (1994).
Coraggio I, Martegani E, Compagno C, Porro D, Alberghiina L, Bernard L, Faoro F, Viotti A: Differential targeting and accumulation of normal and modified zein polypeptides in transformed yeast. Eur J Cell Biol 47: 165–172. (1988).
Coughlan SJ, Hastings C, Winfrey Jr. R: Cloning and characterization of the calreticulin gene from Ricinus communis L. Plant Mol Biol 34: 897–911 (1997).
Cox JS, Chapman RE, Walter P: The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane. Mol Biol Cell 8: 1805–1814 (1997).
Cox JS, Shamu CE, Walter P: Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73: 1197–1206 (1993).
Cox JS, Walter P: A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87: 391–404 (1996).
Craven RA, Egerton M, Stirling CJ: A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors. EMBO J 15: 2640–2650 (1996).
Crowley KS, Reinhart GD, Johnson AE: The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation. Cell 73: 1101–1115 (1993).
D’Amico L, Valsasina B, Daminati MG, Fabbrini MS, Nitti G, Bollini R, Ceriotti A, Vitale A: Bean homologs of the mammalian glucose-regulated proteins: induction by tuni-camycin and interaction with newly synthesized seed storage proteins in the endoplamic reticulum. Plant J 2: 443–455 (1992).
De Loose M, Gheysen G, Tire C, Gielen J, Villarroel R, Genetello C, Van Montagu M, Depicker A, Inzé D: The extensin signal peptide allows secretion of a heterologous protein from protoplasts. Gene 99: 95–100 (1991).
Denecke J: Soluble endoplasmic reticulum resident proteins and their function in protein synthesis and transport. Plant Physiol Biochem 34: 197–205 (1996).
Denecke J, Botterman J, Deblaere R: Protein secretion in plant cells can occur via a default pathway. Plant Cell 2: 51–59 (1990).
Denecke J, Carlsson LE, Vidal S, Hoglund AS, Ek B, Van Zeijl MJ, Sinjorgo KM, Palva ET: The tobacco homolog of mammalian calreticulin is present in protein complexes in vivo. Plant Cell 7: 391–406 (1995).
Denecke J, Goldman MHS, Demolder J, Seurinck J, Botterman J: The tobacco luminal binding protein is encoded by a multigene family. Plant Cell 3: 1025–1035 (1991).
Deshaies RJ, Koch BD, Werner-Washburne M, Craig E, Sheckman R: A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332: 800–805 (1988).
Dickinson CD, Floener LA, Lilley GG, Nielsen NC: Self-assembly of proglycinin and hybrid proglycinin synthesized in vitro from cDNA. Proc Natl Acad Sci USA 84: 5525–5529 (1987).
Dierks T, Volkmer J, Schlenstedt G, Jung C, Sandholzed U, Zchman K, Schlotterhose P, Neifer K, Schmidt B, Zimmermann R: A microsomal ATP-binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum. EMBO J 15: 6931–6942 (1996).
Dresselhaus T, Hagel C, Lorz H, Kranz E: Isolation of a full-length cDNA encoding calreticulin from a PCR library of in vitro zygotes of maize. Plant Mol Biol 31: 23–24 (1996).
Esen A, Stetler DA: Immunocytochemical localization of δ-zein in the protein bodies of maize endosperm cells. Am Bot 79:243–248 (1992).
Essex DW, Chen K, Swiatkowska M: Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane. Blood 15: 2168–2173 (1995).
Evans EA, Gilmore R, Blobel G: Purification of microsomal signal peptidase as a complex. Proc Natl Acad Sci USA 83: 581–585 (1986).
Firek S, Draper J, Owen MRL, Gandecha A, Cockburn B, Withelam GC: Secretion of a functional single-chain Fv protein in transgenic tobacco plants and cell suspension cultures. Plant Mol Biol 23: 861–870 (1993).
Fitchette-Lainé A-C, Denmat L-A, Lerouge P, Faye L: Analysis of N-and O-glycosylation of plant proteins. In: Cunningham C, Porter A (eds) Methods in Biotechnology, Recombinant Proteins from Plants: Production and Isolation of Clinically Useful Compounds, vol. 3, pp. 271–290. Humana Press, Totowa, NJ (1997).
Fitting T, Kabbat D: Evidence for a glycoprotein’ signal’ involved in transport between subcellular organelles. Two membrane glycoproteins encoded by murine leukemia virus reach the cell surface at different rates. J Biol Chem 257: 14011–14017 (1982).
Fontes EBP, Shank BB, Wrobel RL, Moose SP, O’Brian GR, Wurtzel ET, Boston RS: Characterization of an im-munoglobin binding protein homolog in the maize floury-2 endosperm mutant. Plant Cell 3: 483–496 (1991).
Freedman RB: Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins. Cell 57: 1069–1072 (1989).
Freedman RB, Hirst TR, Tuite MF: Protein disulphide isomerase: building bridges in protein folding. Trends Biochem Sci 19:331–336 (1994).
Freskgård P-O, Bergenhem N, Johnson B-H, Svensson M, Carlsson U: Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anydrase. Science 258: 466–468 (1992).
Galili G: The prolamin storage proteins of wheat and its relatives. In: Larkins BA, Vasil IK (eds) Cellular and Molecular Biology of Plant Seed Development, pp. 221–256. Kluwer Academic Publishers, Dordrecht, Netherlands (1997).
Galili G, Altschuler Y, Levanony H: Assembly and transport of seed storage proteins. Trends Cell Biol 3: 437–443 (1993).
Galili G, Giorini-Silfen S, Shimoni Y, Altschuler Y, Levanony H, Shani N, Karchi H, Galun E: Assembly and intracellular transport of wheat storage proteins. J Cell Biochem (Suppl 19A-019): 132 (1995).
Galili G, Shimoni Y, Giorini-Silfen S, Levanony H, Altschuler Y, Shani N: Wheat storage proteins: assembly, transport and deposition in protein bodies. Plant Physiol Biochem 34: 245–252 (1996).
Gallois P, Makishima T, Hecht V, Despres B, Laudié M, Nishimoto T, Cooke R: An Arabidopsis thaliana cDNA complementing a hamster apoptosis suppressor mutant. Plant J 11: 1325–1331 (1997).
Gasser CS, Gunning DA, Budelier KA, Brown SM: Structure and expression of cytosolic cyclophilin/peptidyl-prolyl cis-trans isomerase of higher plants and production of active tomato cyclophilin in Escherichia coli. Proc Natl Acad Sci USA 87: 9519–9523 (1990).
Gavel Y, Von Heijne G: Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. Prot Engng 3: 433–442 (1990).
Geli M, Torrent M, Ludevid D: Two structural domains mediate two sequential events in γ-zein targeting: protein endoplasmic reticulum retention and protein body formation. Plant Cell 6: 1911–1922 (1994).
Gething M-J, Sambrook J: Protein folding in the cell. Nature 355:33–45 (1992).
Gillikin JW, Fontes EPB, Boston RS: Protein-protein interactions within the endoplasmic reticulum. In: Galbraith DW, Bourque DP, Bohnert HJ (eds) Methods in Cell Biology, pp. 309–323. Academic Press, San Diego (1995).
Gillikin JW, Zhang F, Coleman CE, Bass HW, Larkins BA, Boston RS: A defective signal peptide tethers the floury-2 zein to the endoplasmic reticulum membrane. Plant Physiol 114:345–352 (1997).
Gomord V, Denmat LA, Fitchette-Lainé AC, Satiat-Jeunemaitre B, Hawes C, Faye L: The C-terminal HDEL sequence is sufficient for retention of secretory proteins in the endoplasmic reticulum (ER) but promotes vacuolar targeting of proteins that escape the ER. Plant J 2: 313–325 (1997).
Gomord V, Faye L: Signals and mechanisms involved in intracellular transport of secreted proteins in plants. Plant Physiol Biochem 34: 165–182 (1996).
Görlich D, Rapoport TA: Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 75: 615–630 (1993).
Haas IG, Wabl M: Immunoglobulin heavy chain binding protein. Nature 306: 387–389 (1983).
Hamman BD, Chen J-C, Johnson EE, Johnson AE: The aqueous pore through the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane. Cell 89: 535–544 (1997).
Hammond C, Helenius A: Quality control in the secretory pathway. Curr Opin Cell Biol 7: 523–529 (1995).
Hanein D, Matlack KES, Jungnickel B, Plath K, Kalies KU, Miller KR, Rapoport TA, Akey CW: Oiligomeric rings of the Sec61p complex induced by ligands required for protein translocation. Cell 87: 721–732 (1996).
Hann BC, Walter P: The signal recognition particle in S. cerevisiae. Cell 67: 131–144 (1991).
Hart GW, Brew K, Grant GA, Bradshaw RA, Lennarz WJ: Primary structural requirements for the enzymatic formation of the N-glycosidic bond in glycoproteins. Studies with natural and synthetic peptides. J Biol Chem 254: 9747–9753 (1979).
Hartmann E, Rapoport TA, Lodish HF: Predicting the orientation of eukaryotic membrane-spanning proteins. Proc Natl Acad Sci USA 86: 5786–5790 (1989).
Hartmann E, Sommer T, Prehn S, Görlich D, Jentsch S, Rapoport TA: Evolutionary conservation of components of the protein translocation complex. Nature 367: 654–657 (1994).
Hassan A-M, Wesson C, Trumble WR: Calreticulin is the major Ca2+ storage protein in the endoplasmic reticulum of the pea plant (Pisum sativum). Plant Physiol 221: 54–59 (1995).
Hatano K, Shimada T, Hiraiwa N, Nishimura M, Hara-Nishimura I: A rapid increase in the level of binding protein (BiP) is accompanied by synthesis and degradation of storage proteins in pumpkin cotyledons. Plant Cell Physiol 38: 344–351 (1997).
Hayano T, Hirose M, Kikuchi M: Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell. FEBS Lett 377: 505–511 (1995).
Heard DJ, Filipowicz W, Marques JP, Palme K, Gualberto JM: An upstream U-snRNA gene-like promoter is required for transcription of the Arabidopsis thaliana 7SL RNA gene. Nuc Acids Res 23: 1970–1976 (1995).
Hein M, Tang Y, McLeod DA, Janda KD, Hiatt A: Evaluation of immunoglobulins from plant cells. Biotechnol Prog 7: 455–461 (1991).
Helenius A, Trombetta ES, Herbert DN, Simons JF: Calnexin calreticulin and the folding of glycoproteins. Trends Cell Biol 7: 193–200 (1997).
Helm KW, LaFayette PR, Nagao RT, Key JL, Vierling E: Localization of small heat-shock proteins to the higher plant endomembrane system. Mol Cell Biol 13: 238–247 (1993).
Hendershot L, Bole D, Kearney JF: The role of immunoglobulin heavy chain binding protein in immunoglobulin transport. Immunol Today 8: 111–114 (1987).
Hendershot L, Bole D, Kohler G, Kearney JF: Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein. J Cell Biol 104:761–767 (1987).
Hendershot LM: Immunoglobulin heavy chain and binding protein complexes are dissociated in vivo by light chain addition. J Cell Biol 111: 829–837 (1990).
Henderson J, Bauly JM, Ashford DA, Oliver SC, Hawes CR, Lazarus CM, Benis MA, Napier RM: Retention of maize auxin-binding protein in the endoplasmic reticulum: quantifying escape and the role of auxin. Planta 202: 313–323 (1997).
Hendrick JP, Hartle F-U: Molecular chaperone functions of heat-shock proteins. Annu Rev Biochem 62: 349–384 (1993).
Herman EM: Immunogold-localization and synthesis of an oil-body membrane protein in developing soybean seeds. Planta 172: 336–345 (1987).
Herman EM: Multiple origins of intravacuolar protein accumulation in plant cells. In: Malhotra K (eds), Advances in Structural Research, pp. 243–283. JAI Press, Greenwich, CT (1994).
Herman EM: Cell and molecular biology of seed oil development. In: Kigel J, Galili G (eds) Seed Development and Germination, pp. 195–214. Marcel Dekker, New York (1995).
Hesse T, Garbers C, Brzobohaty B, Kreimer G, Söil D, Melkonian M, Schell J, Palme K: Two members of the ERabp family are expressed differentially in reproductive organs but to similar levels in the coleoptile of maize. Plant Mol Biol 23: 57–66 (1993).
Hiatt A, Cafferkey R, Bowdish K: Production of antibodies in transgenic plants. Nature 342: 76–78 (1989).
High S, Andersen SSL, Görlich D, Hartmann E, Prehn S, Rapoport TA, Dobberstein B: Sec61 is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion. J Cell Biol 121: 743–750 (1993).
Hills MJ, Watson MD, Murphy DJ: Targeting of oleosin to the oil bodies of oilseed rape Brassica napus L. Planta 189: 24–29 (1993).
Hoffman LM, Donaldson DD, Bookland R, Rashka K, Herman EM: Synthesis and protein body deposition of maize 15kD zein in transgenic tobacco seeds. EMBO J 6: 3213–3221 (1987).
Hoffman LM, Donaldson DD, Herman EM: A modified storage protein is synthesized, processed, and degraded in the seeds of transgenic plants. Plant Mol Biol 11: 717–729 (1988).
Holland EC, Drickamer K: Signal recognition particle mediates the insertion of a transmembrane protein which has a cytoplasmic NH2 terminus. J Biol Chem 261: 1286–1292 (1986).
Hoist B, Brunn AW, Kielland-Brandt MC, Winther JR: Competition between folding and glycosylation in the endoplasmic reticulum. EMBO J 15: 3538–3546 (1996).
Holwerda BC, Padgett HS, Rojers JC: Proaleurain vacuolar targeting is mediated by short contiguous peptide interactions. Plant Cell 4: 307–318 (1992).
Hong E, Davidson AR, Kaiser CA: A pathway for targeting soluble misfolded proteins to the yeast vacuole. J Cell Biol 135: 623–633 (1996).
Hori H, Kaushal GP, Elbein AD: Biosynthesis of mannose-containing lipid-linked oligosaccharides by solubilized enzyme preparation from cultured soybean cells. Plant Physiol 77: 840–846 (1985).
Hori H, Pan YT, Molyneux RJ, Elbein AD: Inhibition of processing of plant N-Iinked oligosaccharides by castanospermine. Arch Biochem Biophys 228: 525–533 (1984).
Huang AHC: Oleosins and oil bodies in seeds and other organs. Plant Physiol 110: 1055–1061 (1996).
Huang L, Franklin AE, Hoffman NE: Primary structure and characterization of an Arabidopsis thaliana calnexin-like protein. J Biol Chem 268: 6560–6566 (1993).
Hull JD, Gilmore RA, Lamb RA: Integration of a small integral membrane protein, M2, of influenza virus into the endoplasmic reticulum: analysis of the internal signal-anchor domain of a protein with an ectoplasmic NH2 terminus. J Cell Biol 106: 1489–1498 (1988).
Hunt DC, Chrispeels MJ: The signal peptide of a vacuolar protein is necessary and sufficient for the efficient secretion of a cytosolic protein. Plant Physiol 96: 18–25 (1991).
Hwang C, Sinskey AJ, Lodish HF: Oxidized redox state of glutathione in the endoplasmic reticulum. Nature 257: 1496–1502 (1992).
Iturriaga G, Jefferson RA, Bevan MW: Endoplasmic reticulum targeting and glycosylation of hybrid proteins in transgenic tobacco. Plant Cell 1: 381–390 (1989).
Jackson MR, Nilsson T, Peterson PA: Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J 9: 3153–3162 (1990).
John DC, Grant ME, Bulleid NJ: Cell-free synthesis and assembly of prolyl 4-hydroxylase: the role of theβ-subunit (PDI) in preventing misfolding and aggregation of the α-subunit. EMBO J 12: 1587–1595 (1993).
Jones RL: Protein synthesis and secretion by the barley aleurone: a perspective. Israel J Bot 34: 377–395 (1985).
Jung R, Young-Woo N, Saalbach I, Muntz K, Nielsen N: Role of sulfhydryl redox state and disulfide bonds in processing and assembly of 11S seed globulins. Plant Cell 9: 2037–2050 (1997).
Kalies K-U, Görlich D, Rapoport TA: Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex. J Cell Biol 126: 925–934 (1994).
Kalinski A, Rowley DL, Loer DS, Foley C, Buta G, Herman EM: Binding-protein expression is subject to temporal, developmental and stress-induced regulation in terminally differentiated soybean organs. Planta 195: 611–621 (1995).
Kaushal GP, Pastuszak I, Hatanaka K-i, Elbein AD: Purification to homogeneity and properties of glucosidase II from mung bean seedlings and suspension-cultured soybean cells. J Biol Chem 1990: 16271–16279 (1990).
Kaushal GP, Zeng Y, Elbein AD: Biosynthesis of glucosidase II in suspension-cultured soybean cells. J Biol Chem 14536–14542 (1993).
Kelleher D, Kreibich G, Gilmore R: Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kd protein. Cell 69: 55–65 (1992).
Kelleher DJ, Gilmore R: The Saccharomyces cerevisiae oligosaccharyltransferase is a protein complex composed of Wbplp, Swplp and four additional polypeptides. J Biol Chem 269: 12908–12917 (1994).
Kermode AR, Fisher SA, Polishchuk E, Wandelt C, Spencer D, Higgins TJV: Accumulation and proteolytic processing of vicilin deletion-mutant proteins in the leaf and seed of transgenic tobacco. Planta 197: 501–513 (1995).
Kirihara JA, Hunsperger JP, Mahoney WC, Messing JW: Differential expression of a gene for a methionine-rich storage protein in maize. Mol Gen Genet 211: 477–484. (1988).
Klappa P, Zimmermann M, Zimmermann R: The membrane protein TRAMp and Sec6lap may be involved in post-translational transport of presecretory proteins into mammalian microsomes. FEBS Lett 341: 281–287 (1994).
Knittler MR, Haas IG: Interaction of BiP with newly synthesized immunoglobulin light chain molecules: cycles of sequential binding and release. EMBO J 11: 1573–1581 (1992).
Koivu J, Myllyla R, Helaakoski T, Pihlajaniemi T, Tasanen K, Kivirikko KI: A single polypeptide acts both as the β subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase. J Biol Chem 262: 6447–6449 (1987).
Koizumi N: Isolation and responses to stress of a gene that encodes a luminal binding protein in Arabidopsis thaliana. Plant Cell Physiol 37: 862–865 (1996).
Kopito RR: ER quality control: the cytoplasmic connection. Cell 88: 427–430 (1997).
Kornfeld R, Kornfeld S: Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 54: 631–664 (1985).
Kozutsumi Y, Segal M, Normington K, Gething M-J, Sambrook J: The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332: 462 (1988).
Kuehn MJ, Herrmann JM, Scheckman R: COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature 391: 187–190 (1998).
Kuehn MJ, Schekman R: COPII and secretory cargo capture into transport vesicles. Curr Opin Cell Biol 9: 447–483 (1997).
Kwiatkowski BA, Zielinska-Kwiatkowska AG, Migdalski A, Kleczkowski LA, Wasilewska LD: Cloning of two cDNAs encoding calnexin-like and calreticulin-like proteins from maize (Zea mays) leaves: identification of potential calcium-binding domains. Gene 165: 219–222 (1995).
Laboissiere MC, Sturley SL, Raines RT: The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J Biol Chem 270: 28006–28009 (1995).
Lacey DJ, Hills MJ: Heterogeneity of the endoplasmic reticulum with respect to lipid syntheis in developing seeds of Brassica napus L. Planta 199: 545–551 (1996).
LaMantia ML, Lennarz WJ: The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell 74: 899–908 (1993).
Lee DH, Bennett S, Pedersen K: Evidence against a potential endoplasmic reticulum transmembrane domain of 27K zein expressed in Xenopus oocytes. Prot Eng 8: 91–96 (1995).
Lee HI, Gal S, Newman TC, Raikhel NV: The Arabidopsis endoplasmic reticulum retention receptor functions in yeast. Proc Natl Acad Sci USA 90: 11433–11437 (1993).
Lee K, Bih FY, Learn GH, Ting JTL, Sellers C, Huang AHC: Oleosins in the gametophyte of Pinus and Brassica and their phylogenetic relationship with those in the sporophytes of various species. Planta 193: 461–469 (1994).
Lending CR, Larkins BA: Changes in the zein composition of protein bodies during maize endosperm development. Plant Cell 1: 1011–1023 (1989).
Lerouge P, Fitchette-Lainé A-C, Chekkafi A, Avidgor V, Faye L: N-Iinked oligosaccharide processing is not necessary for glycoprotein secretion in plants. Plant J 10: 713–719 (1996).
Levanony H, Rubin R, Altschuler Y, Galili G: Evidence for a novel route of wheat storage proteins in vacuoles. J Cell Biol 119: 117–128 (1992).
Lewis MJ, Pelham HR: A human homologue of the yeast HDEL receptor. Nature 348: 162–163 (1990).
Li CP, Larkins BA: Expression of protein disulfide isomerase is elevated in the endosperm of the maize floury-2 mutant. Plant Mol Biol 30: 873–882 (1996).
Li X, Franceschi VR, Okita TW: Segregation of storage protein mRNAs on the rough endoplasmic reticulum membranes of rice endosperm cells. Cell 72: 869–879 (1993).
Li X, Wu Y, Zhang DZ, Gillikin JW, Boston RS, Franceschi VR, Okita TW: Rice prolamin protein body biogenesis: a BiP-mediated process. Science 262: 1054–1056 (1993).
Lindstrom J, Chu B, Belanger F: Molecular cloning and characterization of an Arabidopsis thaliana gene for the 54 kDa subunit of the signal recognition particle. Plant Mol Biol 23: 1265–1272 (1993).
Lodish HF, Kong N, Snider M, Strous GJAM: Hepatoma secretory proteins migrate from rough endoplasmic reticulum to Golgi at characteristic rates. Nature 304: 80–83 (1983).
Loer DS, Herman EM: Cotranslational integration of soybean (Glycine max) oil body membrane protein oleosin into microsomal membranes. Plant Physiol 101: 993–998 (1993).
Lopes MA, Coleman CE, Kodrzycki R, CR L: Synthesis of an unusual α-zein protein is correlated with the phenotypic effects of floury-2 mutation in maize. Mol Gen Genet 245: 537–547 (1994).
Lord JM: Go outside and see the proteasome. Curr Biol 6: 1067–1069 (1996).
Luan S, Kudla J, Gruissem W, Schreiber SL: Molecular characterization of a FKBP-type immunophilin from higher plants. Proc Natl Acad Sci USA 93: 6964–6969 (1996).
Lund P, Dunsmuir P: A plant signal sequence enhances the secretion of bacterial ChiA in transgenic tobacco. Plant Mol Biol 18: 47–53 (1992).
Lund P, Lee RY, Dunsmuir P: Bacterial chitinase is modified and secreted in transgenic tobacco. Plant Physiol 91: 130–135 (1989).
Lupattelli F, Pedrazzini E, Bollini R, Vitale A: The rate of phaseolin assembly is controlled by the glucosylation state of its N-Iinked oligosaccharide chains. Plant Cell 9: 597–609 (1997).
Marcantonio EE, Amar-Costenec A, Kreibich G: Segregation of the polypeptide translocation apparatus to regions of the endoplasmic reticulum containing ribophorins and ribosomes. II. Rat liver microsomal subtractions contain equimolar amounts of ribophorins and ribosomes. J Cell Biol 99 (1984).
Marocco A, Santucci A, Cerioli S, Motto M, Difonzo N, Thompson R, Salamini F: Three high-lysine mutations control the level of ATP-binding HSP70-like proteins in the maize endosperm. Plant Cell 3: 507–515 (1991).
Marshallsay C, Prehn S, Zwieb C: cDNA cloning of the wheat germ SRP 7S RNAs. Nucl Acids Res 17: 1771 (1989).
Matsuoka K, Watanabe N, Nakamura K: O-Glycosylation of a precursor to a sweet potato vacuolar protein, sporamin, expressed in tobacco cells. Plant J 8: 877–889 (1995).
Maurel C, Kado RT, Guern J, Chrispeels M: Phosphorylation regulates the water channel activity of the seed-specific aquaporin α-TIP. EMBO J 14: 3028–3035 (1995).
Maurel C, Reizer J, Schroeder J, Chrispeels M: The vacuolar membrane protein α-TIP creates water specific channels in Xenopus oocytes. EMBO J 12: 2241–2247 (1993).
McGinnes LW, Morrison TG: Disulfide bond formation is a determinant of glycosylation site usage in the hemagglutinin-neuramidase glycoprotein in Newcastle-Disease virus. J Virol 71: 3083–3089 (1997).
Melnick J, Dul JL, Argon Y: Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature 370: 373–375 (1994).
Menegazzi P, Guzzo F, Baldan B, Mariani P, Treves S: Purification of calreticulin-like protein(s) from spinach leaves. Biochem Biophys Res Comm 190: 1130–1135 (1993).
Meyer DI, Krause E, Dobberstein B: Secretory protein translocation across membranes-the role of the’ docking protein’. Nature 297: 647–650 (1982).
Miernyk JA, Duck NB, Shatters RGJ, Folk WR: The 70-kilodalton heat shock cognate can act as a molecular chaperone during the membrane translocation of a plant secretory protein precursor. Plant Cell 4: 821–829 (1992).
Miyata S, Akazawa T: α-Amylase biosynthesis: evidence for temporal sequence of NH2-terminal peptide cleavage and protein glycosylation. Proc Natl Acad Sci USA 79: 6566–5668 (1982).
Mizuno M, Singer SJ: A soluble secretory protein is first concentrated in the endoplasmic reticulum before transfer to the Golgi apparatus. Proc Natl Acad Sci USA 90: 5732–5736 (1993).
Moore PJ, Swords KMM, Lynch MA, Staehelin LA: Spatial organization of the assembly pathways of glycoproteins and complex polisaccharides in the Golgi apparatus of plants. J Cell Biol 112: 589–602 (1991).
Mori K, Ma W, Gething MJ, Sambrook J: A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell 74: 743–756 (1993).
Mothes W, Heinrich SU, Graf R, Nilsson I, von Heijne G, Brunner J, Rapoport TA: Molecular mechanism of membrane protein integration into the endoplasmic reticulum. Cell 89: 523–533 (1997).
Munro S, Pelham HRB: An hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46: 291–300 (1986).
Munro S, Pelham HRB: A C-terminal signal prevents secretion of luminal ER proteins. Cell 48: 899–907 (1987).
Murphy DJ: Structure, Function and biogenesis of storage lipid bodies and oleosins in plants. Prog Lipid Res 32: 247–280 (1993).
Nam YW, Jung R, Nielsen NC: Adenosine 5’-triphosphate is required for the assembly of 11S seed proglobulins in vitro. Plant Physiol 115: 1629–1639 (1997).
Napier JA, Richard G, Turner MFP, Shewry PR: Trafficking of wheat gluten proteins in transgenic tobacco plants: γ-gliadin does not contain an endoplasmic retention signal. Planta 203: 488–494 (1997).
Napier JA, Stobart AJ, Shewry PR: The structure and biogenesis of plant oil bodies: the role of the ER membrane and the oleosin class of proteins. Plant Mol Biol 31: 945–956 (1996).
Napier RM: Trafficking of the auxin-binding protein. Trends Plant Sci 2: 251–255 (1997).
Napier RM, Trueman S, Henderson J, Boyce JM, Hawes C, Fricker MD, Venis MA: Purification, sequencing and functions of calreticulin from maize. J Exp Bot 46: 1603–1613 (1995).
Nelson DE, Glaunsinger B, Bohnert HJ: Abundant accumulation of the calcium-binding molecular chaperone calreticulin in specific floral tissues of Arabidopsis thaliana. Plant Physiol 114: 29–37 (1997).
Nielsen H, Engelbrecht J, Brunak S, von Heijne G: Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Prot Eng 10: 1–6 (1997).
Nielsen NC, Jung R, Nam Y, Beaman TW, Oliveira LO, Bassuner RB: Synthesis and assembly of 11S globulins. J Plant Physiol 145: 641–647 (1995).
Nilsson I-M, von Heijne G: Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J Biol Chem 268: 5798–5801 (1993).
Noiva R, Freedman RB, Lennarz WJ: Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites. J Biol Chem 268: 19210–19217 (1993).
Noiva R, Lennarz WJ: Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum. J Biol Chem 267: 3553–3556 (1992).
Okamoto T, Nakayama H, Seta K, Isobe T, Minamikawa T: Posttranslational processing of a carboxy-terminal propeptide containing a KDEL sequence of plant vacuolar cysteine endopeptidase (SH-EP). FEBS Lett 351: 31–34 (1994).
Okita TW, Li X, Roberts MW: Targeting of mRNAs to domains of the endoplasmic reticulum. Trends Cell Biol 4: 91–96 (1994).
Okita TW, Rogers JC: Compartmentation of proteins in the endomembrane system in plant cells. Annu Rev Plant Physiol Plant Mol Biol 47: 327–350 (1996).
Olden K, Paratt RM, Jaworski C, Yamada K: Evidence for role of glycoprotein carbohydrates in membrane transport: specific inhibition by tunicamycin. Proc Natl Acad Sci USA 76: 791–795 (1979).
Ori N, Sessa G, Lotan T, Himmelhoch S, Fluhr R: A major stylar matrix polypeptide (sp41) is a member of the pathogenesis-related proteins superclass. EMBO J 9: 3429–3436 (1990).
Osborne TB: The Vegetable Proteins. Longmans, Green and Co., London (1924).
Pahl H, Baeuerle PA: Endoplasmic-reticulum-induced signal transduction and gene expression. Trends Cell Biol 7: 50–55 (1997).
Pang SZ, Rasmussen J, Ye GN, Sanford JC: Use of the signal peptide of Pisum vicilin to translocate β-glucuronidase in Nicotiana tabacum. Gene: 229–234 (1992).
Panzner S, Dreier L, Hartmann E, Kostka S, Rapoport T: Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 81: 561–570 (1995).
Parodi AJ, Mendelzon DH, Lederkremer GH, MartÃn-Barrientos J: Evidence that transient glucosylation of protein-linked Man9GlcNAc2, Man8GlcNAc2 and Man7GlcNAc2occurs in rat liver and Phaseolus vulgaris cells. J Biol Chem 259: 6351–6357 (1984).
Pedrazzini E, Giovinazzo G, Bielli A, de Virgilio M, Frigerio L, Pesca M, Faoro F, Bollini R, Ceriotti A, Vitale A: Protein quality control along the route to the plant vacuole. Plant Cell 9: 10 (1997).
Pedrazzini E, Giovinazzo G, Bollini R, Ceriotti A, Vitale A: Binding of BiP to an assembly-defective protein in plant cells. Plant J 5: 103–110 (1994).
Pedrazzini E, Vitale A: The binding protein (BiP) and the synthesis of secretory proteins. Plant Physiol Biochem 34: 207–216 (1996).
Pelham HR: Sorting and retrieval between the endoplasmic reticulum and Golgi apparatus. Curr Opin Cell Biol 7: 530–535 (1995).
Pelham HRB: Control of protein exit from the endoplasmic reticulum. Annu Rev Cell Biol 5: 1–23 (1989).
Pelham HRB: The retention signal for soluble proteins of the endoplasmic reticulum. Trends Biochem Sci 15: 483–486. (1990).
Poruchynsky MS, Atkinson PH: Primary sequence domains required for the retention of rotavirus VP7 in the endoplasmic reticulum. J Cell Biol 107: 1697–706 (1988).
Prehn S, Wiedmann M, Rapoport TA, Zwieb C: Protein translocation across wheat germ microsomal membranes requires an SRP-Iike component. EMBO J 6: 2093–2097 (1987).
Pueyo JU, Chrispeels MJ, Herman EM: Degradation of transport-competent destabilized phaseolin with a signal for retention in the endoplasmic reticulum occurs in the vacuole. Planta 196: 586–596 (1995).
Rapoport TA, Jungnickel B, Kutay U: Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu Rev Biochem 65: 271–303 (1996).
Reiss G, te Heesen S, Gilmore R, Zufferey R, Aebi M: A specific screen for oligosaccharyltransferase mutations identifies the 9 kDa OST5 protein required for optimal activity in vivo and in vitro. EMBO J 16: 1164–1172 (1997).
Restrepo-Hartwig MA, Carrington JC: The tobacco etch potyvirus 6kD protein is membrane-associated and involved in viral replication. J Virol 68: 2388–2397 (1994).
Riedel L, Pütz A, Hauser M-T, Luckinger R, Wassenegger M, SϤnger HL: Characterization of the signal recognition particle (SRP) RNA population of tomato (Lycopersicon esculentum). Plant Mol Biol 27: 669–680 (199
Romisch K, Ali BRS: Similar processes mediate glycopeptide export from the endoplasmic reticulum in mammalian cells and Saccharomyces cerevisiae. Proc Natl Acad Sci USA 94: 6730–6734 (199
Romisch K, Schekman R: Distinct processes mediate glycoprotein and glycopeptide export from the endoplasmic reticulum in Sacchawmyces cerevisiae. Proc Natl Acad Sci USA 89: 7227–7231 (1992).
Rosenberg N, Shimoni Y, Altschuler Y, Levanony H, Volokita N, Galili G: Wheat (Triticum aestivum L.) γ-gliadin accumulates in dense protein bodies within the endoplasmic reticulum of yeast. Plant Physiol 102: 61–69 (1993).
Rothman JE: Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell 59: 591–601 (1989).
Sarmiento C, Ross JHE, Herman E, Mirphy DJ: Expression and subcellular targeting of a soybean oleosin in transgenic rapeseed. Implications for the mechanism of oil-body formation in seeds. Plant J 11: 783–796 (1997).
Schaad MC, Jensen PE, Carrington JC: Formation of plant RNA virus replication complexes on membranes: role of an endoplasmic reticulum-targeted viral protein. EMBO J 16: 4049–4059 (1997).
Scheele G, Tartakoff A: Exit of nonglycosylated secretory proteins from rough endoplasmic reticulum is asynchronus in the exocrine pancreas. J Biol Chem 260: 926–931 (1985).
Schernthaner MA, Matzke MA, Matzke AJM: Endosperm-specific activity of α zein gene promoter in transgenic tobacco plants. EMBO J 7: 1249–1255. (1988).
Schreiber SL: Chemistry and biology of immunophilins and their immunosuppressive ligands. Science 251: 283–287 (1991).
Schutze M-P, Peterson PA, Jackson MR: An N-terminal double-arginine motif maintains type II membrane proteins in the endoplasmic reticulum. EMBO J 13: 1696–1705 (1994).
Semenza JC, Hardwick KG, Dean N, Pelham HR: ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway. Cell 61: 1349–1357 (1990).
Sengupta C, DeLuca V, Bailey D, Verma DPS: Post-translational processing of 7S and 11S components of soybean storage proteins. Plant Mol Biol 1: 19–34 (1981).
Shatters R, Miernyk J: A zein signal sequence functions as a signal-anchor when fued to maize alcohol dehydrogenase. Biochim Biophys Acta 1068: 179–188 (1991).
Sheldon PS, Venis MA: Purification and characterization of cytosolic and microsomal cyclophilins from maize (Zea mays). Biochem J 315: 965–969 (199
Shewry PR, Napier JA, Tatham AS: Seed storage proteins: structures and biosynthesis. Plant Cell 7: 945–956 (1995).
Shimoni Y, Galili G: Intramolecular disulfide bonds between conserved cysteines in wheat gliadins control their deposition into protein bodies. J Biol Chem 271: 18869–18874 (1996).
Shimoni Y, Zhu X-Z, Levanony H, Segal G, Galili G: Purification, characterization and intracellular localization of glycosylated protein disulfide isomerase from wheat grains. Plant Physiol 108: 327–335. (1995).
Shiu RPC, Pouyssegur J, Pastan I: Glucose depletion accounts for the induction of two transformation-sensitive membrane proteins in Rous sarcoma virus-transformed chick embryo fibroblasts. Proc Natl Acad Sci USA 74: 3840–3844 (1977).
Shorrosh BS, Dixon RA: Molecular cloning of a putative endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatydilinositol-specific phospholipase C. Proc Natl Acad Sci USA 88: 10941–10945 (1991).
Shorrosh BS, Dixon RA: Molecular characterization and expression of an alfalfa protein with sequence similarity to mammalian ERp72, a glucose-regulated endoplasmic reticulum protein containing active site sequences of protein disulphide isomerase. Plant J 2: 51–58 (1992).
Shotwell M, Larkins BA: The biochemistry and molecular biology of seed storage proteins. In: Marcus E (ed) The Biochemistry of Plants: A Comprehensive Treatise, pp. 296–345. Academic Press, Orlando, FL (1989).
Showalter AM: Structure and function of plant cell wall proteins. Plant Cell 5: 9–23 (1993).
Sijmons PC, Dekker BMM, Schrammeijer B, Verwoerd TC, van den Elzen PJM, Hoekema A: Production of correctly processed human serum albumin in transgenic plants. Bio/technology 8: 217–221 (1990).
Silberstein S, Gilmore R: Biochemistry, molecular biology, and genetics of the oligosaccharyltransferase. FASEB J 10: 849–858 (1996).
Smith MA, Stobart AK, Shewry PR, Napier JA: Tobacco eytochrome b5: cDNA isolation, expression analysis and in vitro protein targeting. Plant Mol Biol 25: 527–537 (1994).
Sommer T, Wolf D: Endoplasmic reticulum degradation: reverse protein flow of no return. FASEB J 11: 1227–1233 (1997).
Sousa M, Ferrero-Garcia MA, Parodi AJ: Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry 31: 97–105 (1992).
Sousa M, Parodi A: The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J 14: 4196–4203 (1995).
Spiess M: Heads or tails: what determines the orientation of proteins in the membrane. FEBS Lett 369: 76–79 (1995).
Staehelin LA: The plant ER: a dynamic organelle composed of a large number of discrete functional domains. Plant J 11: 1151–1165 (1997).
Staehelin LA, Driouich A: Brefeldin A effects in plants. Plant Physiol 114: 401–403 (1997).
Sturm A: N-glycosylation of plant proteins. In: Montreuil J, Schachter H, Vliegenthart JFG (eds) Glycoproteins, pp. 521–541. Elsevier Science, Amsterdam (1995).
Sturm A, Chrispeels MJ, Wieruzeski JM, Strecker G, Montreuil J: Structural analysis of the N-linked oligosaccharides from jack bean α-mannosidase. In: Montreuil J, Verbert G, Spik G and Fournet B (eds) Glycoconjugates: Proceedings of the 9th International Symposium on Glycoconjugates, Lille, France, p. A107 (1987).
Sturm A, Johnson KD, Szumilo T, Elbein AD, Chrispeels MJ: Subcellular localization of glycosidases and glycosyl-transferases involved in the processing of N-Iinked oligosaccharides. Plant Physiol 85: 741–745 (1987).
Szumilo T, Kaushal GP, Elbein AD: Purification and properties of glucosidase I from mung bean seedlings. Arch Biochem Biophys 247: 261–271 (1986).
Tatu U, Helenius A: Interactions between newly synthesized glycoproteins, calnexin, and a network of resident chaper-ones in the endoplasmic reticulum. J Cell Biol 136: 555–565 (1997).
Thoyts pJE, M.I. M, Stobart AK, Griffiths WT, Shewry PR, Napier JA: Expression and in vivo targeting of a sunflower oleosin. Plant Mol Biol 29: 403–410 (1995).
Tooze J, Kern HF, Fuller SD, Howell KE: Condensation-sorting events in the rough endoplasmic reticulum of exocrine pancreatic cells. J Cell Biol 109: 35–50 (1989).
Torrent M, Geli MI, Ruiz-Avila L, Canals MJ, Puigdmenech P, Ludevid D: Role of structural domains for maizey γ-zein retention in Xenopus oocytes. Planta 192: 512–518 (1994).
Trombetta SE, Parodi AJ: Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:glycoprotein glucosyltransferase. J Biol Chem 267: 9236–9240 (1992).
Tzen JTC, Cao YZ, Ratnayake C, Huang AHC: Lipids protein and structure of seed oil bodies from diverse species. Plant Physiol 101: 267–276 (1993).
van Hoist G-J, Fincher GB: Polyprolin II conformation in the protein component of arabinogalactan-protein from Lolium multiflorum. Plant Physiol 75: 1163–1164 (1984).
van Hoist G-J, Varner JE: Reinforced polyproline II conformation in a hydroxyproline-rich cell wall glycoprotein from carrot root. Plant Physiol 74: 247–251 (1984).
Vitale A, Bielli A, Ceriotti A: The binding protein associates with monomeric phaseolin. Plant Physiol 107: 1411–1418 (1995).
Vitale A, Bollini R: Legume storage proteins. In: Kigel H, Galili G (eds) Seed Development and Germination, pp. 73–102. Marcel Dekker, New York (1995).
Vitale A, Ceriotti A, Denecke J: The role of the endoplasmic reticulum in protein synthesis, modification and intracellular transport. J Exp Bot 44: 1417–1444 (1993).
Vogel JP, Misra LM, Rose MD: Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast. J Cell Biol 110: 1885–1895 (1990).
von Heijne G: Signal sequences. The limits of variation. J Mol Biol 184: 99–105 (1985).
Wada K, Buchanan BB: Purothionin: a seed protein with thioredoxin activity. FEBS Lett 124: 237–240 (1981).
Wahlberg JM, Spiess M: Multiple determinants direct the orientation of signal-anchor proteins: the topogenic role of the hydrophobic signal domain. J Cell Biol 137: 555–562 (1997).
Walter P, Blobel G: Translocation of proteins across the endoplasmic reticulum II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein. J Cell Biol 91: 551–556 (1981).
Walter P, Blobel G: Translocation of proteins across the endoplasmic reticulum. 111. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes. J Cell Biol 91: 557–561 (1981).
Wang CC, Tsou CL: Protein disulfide isomerase is both an enzyme and a chaperone. FASEB J 7: 1515–1517 (1993).
Wanker EE, Sun Y, Savitz AJ, Meyer DI: Functional characterization of the 180 kDa ribosome receptor in vivo. J Cell Biol 130: 29–39 (1995).
Wessels HP, Spiess M: Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence. Cell 55: 61–70 (1988).
Wickner G, Lodish HF: Multiple mechanisms of protein insertion into and across membranes. Science 230: 400–407 (1985).
Wieland FT, Cleason ML, Serafini TA, Rothman JE: The rate of bulk flow from the endoplasmic reticulum to the cell surface. Cell 50: 289–300 (1987).
Wolin SL, Walter P: Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate. J Cell Biol 109: 2617–2622 (1989).
Yamauchi D, Akasofu H, Minamikawa T: Cysteine endopeptidase from Vigna mungo: gene structure and expression. Plant Cell Physiol 33: 789–797 (1992).
Zhang F, Boston RS: Increases in binding protein (BiP) accompany changes in protein body morphology in three high-lysine mutants of maize. Protoplasma 171: 142–152 (1992).
Zimmerman DL, Walter P: Reconstitution of protein translocation activity from partially solubilized microsomal vesicles. J Biol Chem 265: 4048–4053 (1990).
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Galili, G., Sengupta-Gopalan, C., Ceriotti, A. (1998). The endoplasmic reticulum of plant cells and its role in protein maturation and biogenesis of oil bodies. In: Soll, J. (eds) Protein Trafficking in Plant Cells. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5298-3_1
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