Adler K, Müntz K: Origin and development of protein bodies in cotyledons of Vicia faba. Planta 157: 401–410 (1983).
Ahmed SU, Bar-Peled M, Raikhel NV: Cloning and subcellular location of an Arabidopsis receptor-like protein that shares common features with protein-sorting receptors of eukaryotic cells. Plant Physiol 114: 325–336 (1997).
Ahmed SU, Bar-Peled M, Raikhel NV: Cloning and subcellular location of an Arabidopsis receptor-like protein that shares common features with protein-sorting receptors of eukaryotic cells. Addendum. Plant Physiol 115: 311–312 (1997).
Altschuler Y, Rosenberg N, Harel P, Galili, G: The Nterminal and C-terminal regions regulate the transport of wheat gliadin through the endoplasmic reticulum in Xenopus oocytes. Plant Cell 5: 443–450 (1993).
Badenoch-Jones J, Spencer D, Higgins TJV, Millerd A: The role of glycosylation in storage-protein synthesis in developing pea seeds. Planta 153: 201–209 (1981).
Bagga S, Adams HP, Rodriguez FD, Kemp JD, Sengupta-Gopalan C: Coexpression of 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).
Bar-Peled M, Bassham DC, Raikhel NV: Transport of proteins in eukaryotic cells: more questions ahead. Plant Mol Biol 32: 223–249 (1996).
Barton KA, Thompson JF, Madison JT, Rosenthal R, Jarvis NP, Beachy RN: The biosynthesis and processing of high molecular weight precursors of soybean glycinin subunits. J Biol Chem 257: 6089–6095 (1982).
Bassüner R, Huth A, Manteuffel R, Rapoport TA: Secretion of globulin polypeptides of Vicia faba by Xenopus leavis oocytes. Eur J Biochem 133: 321–326 (1983).
Bassüner R, Manteuffel R, Müntz K, Püchel M, Schmidt P, Weber E: Analysis of in vivo and in vitro globulin formation during cotyledon development of field bean (Vicia faba L. var. minor). Biochem Physiol Pflanzen 178: 664–684 (1983).
Bassüner R, Wobus U, Rapoport TA: Signal recognition particle triggers the translation of storage globulin polypeptides from field bean (Vicia faba L.) across mammalian endoplasmic reticulum membrane. FEBS Lett 166: 314–320 (1984).
Becker C, Shutov AD, Nong VH, Senyuk VI, Jung R, Horstmann C, Fischer J, Nielsen NC, Müntz K: Purification, cDNA cloning, and characterization of proteinase B, an asparagine-specific endopeptidase from germinating vetch (Vicia sativa L.) seeds. Eur J Biochem 228: 456–462 (1995).
Bergfeld R, Kühnl T, Schopfer P: Formation of protein storage bodies during embryogenesis in cotyledons of Sinapis alba L. Planta 148: 146–156 (1980).
Bollini R, Ceriotti A, Daminati MG, Vitale A: Glycosylation is not needed for intracellular transport of phytohemagglutinin in developing Phaseolus vulgaris cotyledons and for maintenance of its biological activity. Physiol Plant 65: 15–22 (1985).
Bollini R, Chrispeels MJ: Characterization and subcellular localization of vicilin and phytohemagglutinin, the two major reserve proteins of Phaseolus vulgaris. Planta 142: 291–298 (1978).
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).
Boston RS, Viitanen PV, Vierling E: Molecular chaperones and protein folding in plants. Plant Mol Biol 32: 191–222 (1996).
Bowles DJ, Marcus SE, Pappin DJC, Findlach J BC, Eliopoulus E, Maycox PR, Burgess J: Posttranslational processing of concanavalin A precursors in jackbean cotyledons. J Cell Biol 102: 1284–1297 (1986).
Bowles DJ, Pappin DJ: Traffic and assembly of concanavalin A. Trends Biochem Sci 13: 60–64 (1988).
Bulleid NJ, Freedman RB: The transcription and translation in vitro of individual cereal storage proteins genes from wheat (Triticum aestivum cv. Chinese Spring). Evidence for translocation of the translation product and disulfide-bond formation. Biochem J 254: 805–810 (1988).
Bulleid NJ, Freedman RB: Defective co-translational formation of disulfide bonds in protein disulfide isomerase deficient microsomes. Nature 335: 649–651 (1988).
Cameron-Mills V, Ingversen J, Brandt A: Tranfer of in vitro synthesized barley endosperm proteins into the lumen of the endoplasmic reticulum. Carlsberg Res Commun 43: 91–102 (1978).
Cameron-Mills V, Madrid SM: The signal peptide cleavage site of B1 hordein determined by radiosequencing of the in vitro synthesized and processed polypeptide. Carlsberg Res Commun 54: 181–192 (1989).
Cameron-Mills V, von Wettstein D: Protein body formation in the developing barley endosperm. Carlsberg Res Commun 45: 577–594 (1980).
Carrington DM, Auffret A, Hanke DE: Polypeptide ligation occurs during post-translational modification of concanavalin A. Nature 313: 64–67 (1984).
Ceriotti A, Pedrazzini E, Bielli A, Giovinazzo G, Bollini R, Vitale A: Assembly and intracellular transport of phaseolin, the major storage protein of Phaseolus vulgaris L. J Plant Physiol 145: 648–653 (1995).
Ceriotti A, Pedrazzini E, Fabbrini MS, Zoppe M, Bollini R, Vitale A: Expression of the wild-type and mutated vacuolar storage protein phaseolin in Xenopus oocytes reveals relationships between assembly and intracellular transport. Eur J Biochem 202: 959–968 (1991).
Chrispeels MJ, Hartl P, Sturm A, Faye L: Proconcanavalin A is not colinear with concanavalin A and has no lectin activity. J Biol Chem 261: 10021–10024 (1986).
Chrispeels MJ, Higgins TJV, Craig S, Spencer D: Role of endoplasmic reticulum in the synthesis of reserve proteins and the kinetics of their transport to protein bodies in developing pea cotyledons. J Cell Biol 93: 5–14 (1982).
van Cleve B, Apel K: Induction by nitrogen and low temperature of storage protein synthesis in poplar trees exposed to long days. Planta 189: 157–160 (1993).
Coleman CE, Dannenhoffer JM, Larkins BA: The prolamin proteins of maize, sorghum and Coix. In: Larkins BA, Vasil IK (eds) Cellular and Molecular Biology of Plant Seed Development, pp. 257–288. Kluwer Academic Publishers, Dordrecht, Netherlands (1997).
Coleman CE, Herman EM, Takasaki K, Larkins BA: The maize 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, Gillikein JW, Boston RS, Larkins BA: A defective signal peptide in the maize high-lysine mutant fleury-2. Proc Natl Acad Sci USA 92: 6828–6831 (1995).
Coulson AFW: A proposed structure for 'family 18' chitinases. A possible function of narbonin. FEBS Lett 354: 41–44 (1994).
Craig S: Structural aspects of protein accumulation in developing legume seeds. Biochem Physiol Pflanzen 183: 159–171 (1988).
Craig S, Goodchild DJ, Hardham AR: Structural aspects of protein accumulation in developing pea cotyledons. I Qualitative and quantitative changes in parenchyma cell vacuoles. Aust J Plant Physiol 6: 81–98 (1979).
Cunnigham SM, Volonec JJ: Purification and characterization of vegetative storage proteins from alfalfa (Medicago sativa L.) taproots. J Plant Physiol 147: 625–632 (1996).
D'Amico L, Valsasina B, Daminati MG, Fabbrini S, Nitti G, Bollini R, Ceriotti A, Vitale A: Bean homologs of the mammalian glucose-regulated proteins: induction by tunicamycin and interaction with newly synthesized seed storage proteins in the endoplasmic reticulum. Plant J 2: 443–455 (1992).
D'Hondt K, Bosch D, Van Damme J, Goethals M, Vandekerckhove J, Krebbers E: An aspartic proteinase present in seeds cleaves Arabidopsis 2S albumin precursors in vitro. J Biol Chem 268: 20884–20891 (1993).
D'Hondt K, Van Damme J, Van Den Bossche C, Leejeerajumnean S, De Rycke R, Derksen J, Vandekerckhove J, Krebbers E: Studies of the role of the propeptides of the Arabidopsis thaliana 2S albumin. Plant Physiol 102: 425–433 (1993).
Dickinson CD, Floener LA, Lilley GG, Nielsen NC: Selfassembly of proglycinin and hybrid proglycinin synthesized in vitro from cDNA. Proc Natl Acad Sci USA 84: 4425–5529 (1987).
Dickinson CD, Hussein EHA, Nielsen NC: Role of posttranslational cleavage in glycinin assembly. Plant Cell 1: 459–469 (1989).
Duranti M, Guerrieri N, Cerletti P, Vecchio G: The legumin presursor from white lupin seed. Identity of the subunits, assembly and proteolysis. Eur J Biochem 206: 941–947 (1992).
Duranti M, Guerrieri N, Takahashi T, Cerletti P: The legumin-like storage protein of Lupinus albus seeds. Phytochemistry 27: 15–23 (1988).
Duranti M, Horstmann C, Gilroy J, Croy RRD: The molcular basis of N-glycosylation in the 11S globulin (legumin) of lupin seeds. J Protein Chem 14: 107–110 (1995).
Ericson ML, Rödin J, Lenman M, Glimelius K, Josefsson LG, Rask L: Structure of rapeseed 1.7S storage protein, napin, and its precursor. J Biol Chem 261: 14576–14581 (1986).
Faye L, Chrispeels MJ: Transport and processing of the glycosylated precursor of concanavalin A in jackbean. Planta 170: 217–224 (1987).
Faye L, Fitchette-Laine A-C, Gomord V, Chekkafi A, Delauney A-M, Driouich A: Detection, biosynthesis and some functions of glycans N-linked to plant secreted proteins. In: Battey NH, Dickinson HG, Hetherington AM (eds) Post-Translational Modifications in Plants, pp. 213–242. Cambridge University Press, Cambridge, UK (1993).
Galili G: The prolamin storage proteins of wheat and its relatives. In: Larkins BA, Vasil IK (eds) Cellular and Molecular Biologiy 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: 437–442 (1993).
Galili G, Sengupta-Gopalan C, Ceriotti A: The endoplasmic reticulum of plant cells and its role in maturation of secretory proteins and biogenesis of oil bodies. Plant Mol Biol (this issue) (1998).
Gatehouse JA, Lycett GW, Croy RRD, Boulter D: The posttranslational proteolysis of the subunits of vicilin from pea (Pisum sativum L.). Biochem J 207: 629–632 (1982).
Gatehouse JA, Lycett GW, Delauney AJ, Croy RR D, Boulter D: Sequence specificity of the post-translational proteolytic cleavage of vicilin, a seed storage protein of pea (Pisum sativum L.). Biochem J 212: 427–432 (1983).
Geli MI, Torrent M, Ludevid D: Two structural domains mediate two sequential events in-zein targeting: Protein endoplasmic retention and protein body formation. Plant Cell 12: 1911–1922 (1994).
Gomez L, Chrispeels MJ: Tonoplast and soluble vacuolar proteins are targeted by differential mechanisms. Plant Cell 5: 1113–1124 (1993).
Grimwade B, Tatham AS, Freedman RB, Shewry PR, Napier JA: Comparison of the expression patterns of genes coding for wheat gluten proteins and proteins involved in the secretory pathway in developing caryopses of wheat. Plant Mol Biol 30: 1067–1073 (1996).
Hara-Nishimura I: Introduction of a disulfide bond in proglobulin molecules during the 11S globulin biosynthesis in endoplasmic reticulum of developing pumpkin cotyledons. Agric Biol Chem 51: 2007–2008 (1987).
Hara-Nishimura I, Inoue K, Nishimura M: A unique vacuolar processing enzyme responsible for conversion of several protein precursors into mature forms. FEBS Lett 294: 89–93 (1991).
Hara-Nishimura I, Kinoshita T, Hiraiwa N, Nishimura M: Vacuolar processing enzyme in protein-storage vacuole and lytic vacuoles. J Plant Physiol 152: 668–674 (1998).
Hara-Nishimura I, Nishimura M: Proglobulin processing enzyme in vacuoles isolated from developing pumpkin cotyledons. Plant Physiol 85: 440–445 (1987).
Hara-Nishimura I, Shimada T, Hiraiwa N, Nishimura M: Vacuolar processing enzyme responsible for maturation of seed proteins. J Plant Physiol 145: 632–640 (1995).
Hara-Nishimura I, Takeuchi Y, Inoue K, Nishimura M: Vesicle transport and processing of the precursor to 2S albumin in pumpkin. Plant J 4: 793–800 (1993).
Hara-Nishimura I, Takeuchi Y, Nishimura M: Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase from Schistosoma mansoni. Plant Cell 5: 1651–1659 (1993).
Hattori T, Ichihara S, Nakamura K: Processing of a plant vacuolar protein precursor in vitro. Eur J Biochem 166: 533–538 (1987).
Hattori T, Nakagawa T, Maeshima M, Nakamura K, Asahi T: Molecular cloning and nucleotide sequence of cDNA for sporamin, the major soluble protein of sweet potato tuberous root. Plant Mol Biol 5: 3134–320 (1985).
Herman E: Multiple origins of intravacuolar protein accumulation of plant cells. Adv Struct Bot 3: 244–283 (1994).
Herman EM, Shannon LM, Chrispeels MJ: Concanavalin A is synthesized as a glycoprotein precursor. Planta 165: 23–29 (1985).
Hinz G, Menze A, Hohl I, Vaux D: Isolation of prolegumin from developing pea seeds: its binding to endomembranes and assembly into prolegumin hexamers in the protein storage vacuole. J Exp Bot 48: 139–149 (1997).
Hiraiwa N, Kondo M, Nishimura M, Hara-Nishimura I: An aspartic proteinase is involved in the breakdown of propeptides of storage proteins in protein storage vacuoles. Eur J Biochem 246: 133–141 (1997).
Hiraiwa N, Nishimura M, Hara-Nishimura I: Expression and activation of the vacuolar processing enzyme in Saccharomyces cerevisiae. Plant J 12: 819–830 (1997).
Hiraiwa N, Takeuchi Y, Nishimura M, Hara-Nishimura I: A vacuolar processing enzyme in maturing and germinating seeds: its distribution and association changes during development. Plant Cell Physiol 34: 1197–1204 (1993).
Hoffman LM, Donaldson DD, Bookland R, Rashka K, Herman EM: Synthesis and protein body deposition ofmaize 15– kd zein in transgenic tobacco seeds. EMBO J 6: 3213–3221 (1987).
Hoh B, Hinz G, Jeong B-K, Robinson DG: Protein storage vacuoles form de novo during pea cotyledon development. J Cell Sci 108: 299–310 (1995).
Hohl I, Robinson DG, Chrispeels MJ, Hinz G: Transport of storage proteins to the vacuole is mediated by vesicles without a clathrin coat. J Cell Sci 109: 2539–2550 (1996).
Holwerda BC, Rogers JC: Structure, functional properties and vacuolar targeting of the barley thiol protease, aleurain. J Exp Bot 44 (Suppl): 321–229 (1993).
Hurkman WJ, Smith LD, Richter J, Larkins BA: Subcellular compartmentalization of maize storage proteins in Xenopus oocytes injected with zein messenger RNAs. J Cell Biol 89: 292–299 (1981).
Ishii S: Legumain: Asparaginyl endopeptidases. Meth Enzymol 244: 604–615 (1994).
Jung R, Nam Y-W, Saalbach I, Müntz K, Nielsen NC: Role of sulfhydryl redox state and disulfide bonds in processing and assembly of 11S seed globulins. Plant Cell 9: 2037–2050 (1997).
Jung R, Saalbach G, Nielsen NC, Müntz K: Site-specific limited proteolysis of legumin chloramphenicol acetyl transferase fusions in vitro and in transgenic tobacco seeds. J Exp Bot 44 (Suppl): 343–349 (1993).
Jung R, Scott MP, Nam Y-W, Beaman TW, Bassüner R, Saalbach I, Müntz K, Nielsen NC: The role of proteolysis in the processing and assembly of 11S globulins. Plant Cell 10: 343–357 (1998).
Kim WT, Franceschi VR, Krishnan HB, Okita TW: Formation of wheat protein bodies: Involvement of the Golgi apparatus in gliadin transport. Planta 176: 173–182 (1988).
Kirsch T, Paris N, Butler JM, Beevers L, Rogers JR: Purification and initial characterization of a potential plant vacuolar targeting receptor. Proc Natl Acad Sci USA 91: 3403–3407 (1994).
Kirsch T, Saalbach G, Raikhel NV, Beevers L: Interaction of a potential vacuolar targeting receptor with amino-and carboxy-terminal targeting determinants. Plant Physiol 111: 469–474 (1996).
Ko T-P, Ng JD, McPherson A: Three-dimensional structure of canavalin from jack bean (Canavalia ensiformis). Plant Physiol 101: 729–744 (1993).
Koide Y, Hirano H, Matsuoka K, Nakamura K: The Nterminal propeptide of the precursor to sporamin acts as a vacuole-targeting signal even at the C-terminus of the mature part in tobacco cells. Plant Physiol 114: 863–870 (1997).
Krishnan HB, Franceschi VR, Okita TW: Immunochemical studies on the role of the Golgi complex in protein-body formation in rice cells. Planta 169: 471–480 (1986).
Larkins BA, Bracker CE, Tsai CY: Storage protein synthesis in maize. Isolation of zein-synthesizing polysomes. Plant Physiol 57: 740–745 (1976).
Larkins BA, Hurkman WJ: Synthesis and deposition of zein in protein bodies of maize endosperm. Plant Physiol 62: 256–263 (1978).
Larkins BA, Pedersen K, Handa AK, Hurkman WJ, Smith LD: Synthesis and processing of maize storage proteins in Xenopus leavis oocytes. Proc Natl Acad Sci USA 76: 6448–6452 (1979).
Lawrence MC, Izard T, Beuchat M, Blagrove RJ, Colman PM: Structure of phaseolin at a 2.2 Å resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins. J Mol Biol 238: 748–776 (1994).
Lawrence MC, Suzuki E, Varghese JN, Davies PC, Van Donkelaar A, Tulloch PA, Colman PM: The threedimensional structure of the seed storage protein phaseolin at 3 Å resolution. EMBO J 9: 9–16 (1990).
Lerouge P, Cabanes-Macheteau M, Rayon C, Fichette-Laine A-C, Gomord V, Faye L: Glycoprotein biosynthesis in plants: Recent developments and future trends. Plant Mol Biol (this issue) (1998).
Levanony H, Rubin R, Altschuler Y, Galili G: Evidence for a novel route of wheat storage proteins to vacuoles. J Cell Biol 119: 1117–1128 (1992).
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 D-Z, Gillikin GW, Boston RS, Franceschi VR, Okita TW: Rice prolamin protein body biogenesis: a BIP-mediated process. Science 262: 1054–1056 (1993).
Lupattelli F, Pedrazzinin E, Bollinin R, Vitale A: The rate of phaseolin assembly is controlled by the glucosylation state of Nits-linked oligosaccharide chains. Plant Cell 9: 597–609 (1997).
Maeshima M, Sasaki T, Asahi T: Characterization of major proteins in sweet potato tuberous roots. Phytochemistry 24: 1899–1902 (1985).
Marcus SE, Bowles DJ: Deglycosylation of a lectin intermediate during assembly of ConA. Protoplasma 147: 113–116 (1988).
Matsuoka K, Bassham DC, Raikhel NV, Nakamura K: Different sensitivity to wortmannin of two vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells. J Cell Biol 130: 1307–1318 (1995).
Matsuoka K, Matsumoto S, Hattori T, Machida Y, Nakamura K: Vacuolar targeting and post-translational processing of the precursor to the sweet potato tuberous root storage protein in heterologous plant cells. J Biol Chem 265: 19750–19757 (1990).
Matsuoka K, Nakamura K: Propeptide of a precursor to a plant vacuolar protein required for vacuolar targeting. Proc Natl Acad Sci USA 88: 834–838 (1991).
Miflin BJ, Burgess SR: Protein bodies from developing seeds of barley, maize, wheat and peas: the effect of protease treatment. J Exp Bot 33: 251–260 (1982).
Miflin BJ, Burgess SR, Shewry PR: The development of protein bodies in the storage tissues of seeds: subcellular separation of homogenates of barley, maize, and wheat endosperms and of pea cotyledons. J Exp Bot 32: 199–219 (1981).
Muench DG, Okita TW: The storage proteins of rice and oat. In: Larkins BA, Vasil IK (eds) Cellular and Molecular Biology of Plant Seed Development, pp. 289–330. Kluwer Academic Publishers, Dordrecht, Netherlands (1997).
Müntz K: Intracellular protein sorting and the formation of protein reserves in storage tissue cells of plant seeds. Biochem Physiol Pflanzen 185: 315–335 (1989).
Müntz K, Jung R, Saalbach G: Synthesis, processing, and targeting of legume seed proteins. Proc Phytochem Soc Eur 35: 128–146 (1993).
Muren E, Ek B, Björk I, Rask L: Structural comparison of the precursor and the mature form of napin, the 2S storage protein in Brassica napus. Eur J Biochem 242: 214–219 (1996).
Muren E, Rask L: Processing of the 2S storage protein pronapin in Brassica napus and in transformed tobacco. Eur J Biochem 227: 316–321 (1995).
Muren E, Rask L: Processing in vitro of pronapin, the 2S storage protein precursor of Brassica napus produced in a baculovirus expression system. Planta 200: 373–379 (1996).
Nakamura K, Matsuoka K, Mukumoto F, Watanabe N: Processing and transport to the vacuole of a presursor to sweet potato sporamin in transformed tobacco cell line BY-2. J Exp Bot 44 (Suppl): 331–338 (1993).
Napier JA, Richard G, Turner MFP, Shewry PR: Trafficking of wheat gluten proteins in transgenic tobacco plants:γ-gliadin does not contain an endoplasmic reticulum retention signal. Planta 203: 488–494 (1997).
Neuhaus J-M, Rogers JC: Sorting of proteins to vacuoles in plant cells. Plant Mol Biol (this issue) (1998).
zur Nieden U, Manteuffel R, Neumann D, Weber E: Electron microscopic immunocytochemical localization of storage protein in Vicia faba seeds. Eur J Cell Biol 26: 228–233 (1982).
zur Nieden U, Manteuffel R, Weber E, Neumann D: Dictyosomes participate in the intracellular pathway of storage proteins in developing Vicia faba cotyledons. Eur J Cell Biol 34: 9–17 (1984).
Nielsen NC, Bassüner R, Beaman T: The biochemnistry and cell biology of embryo storage proteins. In: Larkins BA, Vasil IK (eds) Cellular and Molecular Biology of Plant Seed Development, pp. 151–221. Kluwer Academic Publishers, Dordrecht, Nethelands (1997).
Okita TW, Rogers JC: Compartmentation of proteins in the endomembrane system of plant cells. Annu Rev Plant Physiol Plant Mol Biol 47: 327–350 (1996).
Osborne TB: The Vegetable Proteins. Monographs in Biochemistry, Longmans, Green and Co, London (1924).
Paris N, Rogers SW, Jiang L, Kirsch T, Beevers L, Phillips TE, Rogers JC: Molecular cloning and further characterization of a probable plant vacuolar sorting receptor. Plant Physiol 115: 29–39 (1997).
Pedrazzini E, Giovinazzo G, Bielli A, Virgilio M de, 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: 1869–1880 (1997).
Pedrazzini E, Giovinazzo G, Bollini R, Ceriotti A, Vitale A: Binding of BIP to assembly-defective protein in plant cells. Plant J 5: 103–110 (1994).
Pedrazzinin E, Vitale A: The binding protein (BIP) and the synthesis of secretory proteins. Plant Physiol Biochem 34: 207–216 (1996).
Püchel M, Müntz K, Parthier B, Aurich O, Bassüner R, Manteuffel R, Schmidt P: RNAmetabolism andmembrane-bound polysomes in relation to globulin biosynthesis in cotyledons of developing field beans. Eur J Biochem 96: 321–324 (1979).
Racusen D: Lipid acyl hydrolase of patatin. Can J Bot 62: 1640–1644 (1984).
Racusen D, Foote M: A major soluble glycoprotein of potato tubers. J Food Biochem 4: 43–52 (1980).
Rechinger KB, Simpson DJ, Svendsen I, Cameron-Mills V: A role for 3–hordein in the transport and targeting of prolamin to the vacuole of developing barley endosperm. Plant J 4: 841–853 (1993).
Robinson DG, Bäumer M, Hinz G, Hohl I: Ultrastructure of the pea Golgi apparatus: origin of dense vesicles and the action of brefeldin A. Protoplasma 200: 198–209 (1997).
Robinson DG, Bäumer M, Hinz G, Hohl I: Vesicle transfer of storage proteins to the vacuole: The role of the Golgi apparatus and multivesicular bodies. J Plant Physiol 152: 659–667 (1998).
Robinson DG, Hinz G: Multiple mechanisms of protein body formation in pea cotyledons. Plant Physiol Biochem 34: 155–163 (1996).
Robinson DG, Hinz G: Vacuole biogenesis and protein transport to the plant vacuole: a comparison with the yeast vacuole and the mammalian lysosome. Protoplasma 197: 1–25 (1997).
Robinson DG, Hinz G, Holstein SEH: The molecular characterization of transport vesicles. Plant Mol Biol (this issue) (1998).
Robinson DG, Hoh B, Hinz G, Jeong B-K: One vacuole or two vacuoles: do protein storage vacuoles arise de novo during pea cotyledon development? J Plant Physiol 145: 654–664 (1995).
Roden LT, Miflin BJ, Freedman RB: Protein disulfide isomerase is located in the endoplasmic reticulum of developing wheat endosperm. FEBS Lett 138: 121–124 (1982).
Rogers JC: Compartmentation of cell proteins in separate lytic and protein storage vacuoles. J Plant Physiol 152: 653–658 (1998).
Rosenberg N, Shimoni Y, Altschuler Y, Levanony H, Volokita M, Galili G: Wheat (Triticum aestivum L.)-gliadin accumulates in dense protein bodies within the endoplasmic reticulum of yeast. Plant Physiol 102: 61–69 (1995).
Saalbach G, Jung R, Kunze G, Saalbach I, Adler K, Müntz K: Different legumin protein domains act as vacuolar targeting signals. Plant Cell 3: 695–708 (1991).
Saalbach G, Rosso M, Schuman U: The vacuolar targeting signal of the 2S albumin from Brazil nut resides at the C-terminus and involves the C-terminal propeptide as an essential element. Plant Physiol 112: 975–985 (1996).
Sauter JJ, van Cleve B: Immunochemical localization of a willow storage protein with a poplar storage protein antibody. Protoplasma 149: 175–177 (1989).
Sauter JJ, van Cleve B, Apel K: Protein bodies in ray cells of Populus Χ canadensis Moench ‘robusta’. Planta 173: 31–34 (1988).
von Schaewen A, Chrispeels MJ: Identification of a vacuolar sorting information in phytohemagglutinin, an unprocessed vacuolar protein. J Exp Bot 44 (Suppl): 339–342 (1993).
Schlesier B, Nong HV, Horstmann C, Hennig M: Sequence analysis of concanavalin B from Canavalia ensiformis reveals homology to chitinases. J Plant Physiol 147. 665–674 (1996).
Schroeder MR, Borkhsenious ON, Matsuoka K, Nakamura K: Colocalization of barley lectin and sporamin in vacuoles of transgenic tobacco. Plant Physiol 101: 451–458 (1993).
Scott MP, Jung R, Müntz K, Nielsen NC: A protease responsible for post-translational cleavage of conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean. Proc Natl Acad Sci USA 89: 658–662 (1992).
Sheldon PS, Bowles DJ: The glycoprotein precursor of concanavalin A is converted to an active lectin by deglycosylation. EMBO J 11: 1297–1302 (1992).
Shewry PR: Plant storage proteins. Biol Rev 70: 375–426 (1995).
Shewry PR, Casey R: Seed proteins. Chapman and Hall, London, in press (1998).
Shewry PR, Napier JA, Tatham AS: Seed storage proteins: structures and biosynthesis. Plant Cell 7: 945–956 (1995).
Shewry PR, Tatham AS: The prolamin storage proteins of cereal seeds: structure and evolution. Biochem J 267: 1–12 (1990).
Shimada T, Hiraiwa N, Nishimura M, Hara-Nishimura I: Vacuolar processing enzyme of soybean that converts proprotein to the corresponding mature forms. Plant Cell Physiol 35: 713–718 (1994).
Shutov AD, Bäumlein H: Origin and evolution of seed storage globulins. In: Shewry PR, Casey R (eds) Seed Proteins, chapter 23. Chapman and Hall, London, in press (1998).
Shutov AD, Kakhovskaya IA, Braun H, Bäumlein H, Müntz K: Legumin-like and vicilin-like seed storage proteins: evidence for a common single-domain ancestral gene. J Mol Evol 41: 1057–1069 (1995).
Simon R, Altschuler Y, Rubin R, Galili G: Two closely related wheat storage proteins follow a markedly different subcellular route in Xenopus leavis oocytes. Plant Cell 2: 941–950 (1990).
Slightom JL, Drong RF, Klassy RC, Hoffman LM: Nucleotide sequences from phaseolin cDNA clones: the major storage proteins from Phaseolus vulgaris are encoded by two unique gene families. Nucl Acids Res 13: 6483–6498 (1985).
Sonnewald U, von Schaewen A, Willmitzer L: Expression of mutant patatin protein in transgenic tobacco plants: role of glycans and intracellular location. Plant Cell 2: 345–355 (1990).
Sonnewald U, Sturm A, Chrispeels MJ, Willmitzer L: Targeting and glycosylation of patatin the major potato tuber protein in leaves of transgenic tobacco. Planta 179: 174–180 (1989).
Staehlin LA: The plant ER: a dynamic organelle composed of a large number of discrete functional domains. Plant J 11: 1151–1165 (1997).
Staswick PE: Soybean vegetative storage protein structure and gene expression. Plant Physiol 87: 250–254 (1988).
Staswick PE: Storage proteins of vegetative plant tissues. Annu Rev Plant Physiol Plant Mol Biol 45: 303–322 (1994).
Staswick PE, Hermodson MA, Nielsen NC: Identification of the cystines which link the acidic and basic components of the glycinin subunits. J Biol Chem 259: 13431–13435 (1984).
Sturm A: N-glycosylation of plant proteins. In: Montreuil J, Schachter H, Vliegenthart JFG (eds) Glycoproteins, pp. 521–541. Comprehensive Biochemistry Vol. 29A. Elsevier, Amsterdam (1995).
Sturm A, Chrispeels MJ: The high mannose oligosaccharide of phytohemagglutinin is attached to asparagine 12 and the modified oligosaccharide to asparagine 60. Plant Physiol 81: 320–322 (1986).
Sturm A, van Kuik JA, Vliegenhart JFG, Chrispeels MJ: Structure, position, and biosynthesis of the high mannose and the complex oligosaccharide side chains of the bean storage protein phaseolin. J Biol Chem 262: 13392–13403 (1987).
Sturm A, Voelker TA, Herman EM, Chrispeels MJ: Correct glycosylation, Golgi-processing, and targeting to protein bodies of the vacuolar protein phytohemagglutinin in transgenic tobacco. Planta 175: 170–183 (1988).
Tague BW, Dickinson CD, Chrispeels MJ: A short domain of the plant vacuolar protein phytohemagglutinin targets invertase to the yeast vacuole. Plant Cell 2: 533–546 (1990).
Thiele C, Gerdes H-H, Huttner WB: Protein secretion: puzzling receptors. Curr Biol 7: R496–R500 (1997).
Torrent M, Geli MJ, Ruiz-Avila L, Canales JM, Puigdomenech P, Ludevid D: Role of structural domains for maize-zein retention in Xenopus oocytes. Planta 192: 512–518 (1994).
Tooze SA: Biogenesis of secretory granules. Implications arising from the immature secretory granule in the regulated pathway of secretion. FEBS Lett 285: 220–224 (1991).
Vitale A, Bielli A, Ceriotti A: The binding protein associates with monomeric phaseolin. Plant Physiol 107: 1411–1418 (1995).
Vitale A, Ceriotti A, Bollini R, Chrispeels MJ: Biosynthesis and processing of phytohemagglutinin in developing bean cotyledons. Eur J Biochem 141: 97–104 (1984).
Vitale A, Chrispeels MJ: Transient N-acetylglucosamine in the biosynthesis of phytohemagglutinin: attachment in the Golgi apparatus and removel in protein bodies. J Cell Biol 99: 133–140 (1984).
Voelker TA, Herman EM, Chrispeels MJ: In vitro mutated phytohemagglutinin genes expressed in tobacco seeds: Role of glycan in protein targeting and stability. Plant Cell 1: 95–104 (1989).
Weber E, Ingversen J, Manteuffel R, Püchel M: Transfer of in vitro synthesized Vicia faba globulins and barley prolamins across the endoplasmic reticulum membrane of Vicia faba. Carlsberg Res Commun 46: 383–393 (1981).
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).