Abstract
Proteins function at distinct sites in a cell, yet they are primarily synthesized in one compartment, the cytosol. (For a concise collection of reviews see (Neupert and Lill, 1992)). This implies that newly synthesized proteins have to be transported to their final destination. Protein transport often involves membrane passage which is a fascinating event because large often polar polypeptide chains of variable composition have to move through an ultra-thin membrane without compromising the other essential barrier function of that membrane.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Billecocq, A (1974) Structures of biological membranes: Localization of galactosyldiglycerides in chloroplasts by means of specific antibodies. Biochim Biophys Acta 352: 245–251
Bulychev, A, Pilon, M, Dassen, H, Van’t Hof, R, Vredenberg, W & De Kruijff, B (1994) Precursormediated opening of translocation pores in chloroplast envelopes. FEBS Lett 356: 204–206
Chupin, V, Van’t Hof, R & De Kruijff, B (1994) The transit sequence-dependent binding of the chloroplast precursor protein ferredoxin to lipid vesicles and its implications for membrane stability. FEBS Lett 350: 104–108
Cornwell, KL & Keegstra, K (1987) Evidence that a chloroplast surface protein is associated with a specific binding site for the precursor to the small subunit of ribulose-l,5-biphosphate carboxylase. Plant Physiol 85: 780–785
Cull is, PR & De Kruijff, B (1979) Lipid polymorphism and the functional roles of lipids in biological membranes. Biochim Biophys Acta 559: 399–420
De Boer, AD & Weisbeek, PJ (1991) Chloroplast topogenesis: Protein import, sorting and assembly.Biochim Biophys Acta 1071: 221–253
Demel, RA, De Swaaf, ME, Mannock, D, Van’t Hof, R & De Kruijff, B (1995) The specificity of glycolipid-preferredoxin interaction. Mol MembrBiol 12: 255–261
Dome, A-J, Joyard, J, Block, MA & Douce, R (1985) Do thylakoids really contain phosphatidylcholine. Proc Natl Acad Sci USA 87: 71–74
Douce, R, Block, MA, Dome, A-J & Joyard, J (1984) The plastid envelope membranes: their structure, composition and role in chloroplast biogenesis. Subcell Biochem 10: 1–84
Douce, R & Joyard, J (1990) Biochemistry and function of the platid envelope. Annu Rev Cell Biol 6: 173–216
Douglas, MG, McCammon, MT & Vassaroti, A (1986) Targeting proteins into mitochondria. Microbiol Rev 50: 166–178
Eilers, M & Schatz, G (1986) Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Nature 322: 228–232
Ellis, RJ (1981) Chloroplast proteins: synthesis, transport and assembly. Annu Rev Plant Physiol 32: 111–137
Endo, T, Kawamura, M & Nakai, M (1992) The chloroplast-targeting domain of a plastocyanin transit peptide can form a helical structure but does not have a high affinity for lipid bilayers. Eur J Biochem 207:671–675
Friedman, AL & Keegstra, K (1989) Quantitative analysis of precursor binding. Plant Physiol 89: 993–-999
Gasser, SM, Daum, G & Schatz, G (1982) Import of proteins into mitochondria. Energy-dependent uptake of precursors by isolated mitochondria. J Biol Chem 257, 13034–13041
Gierash, LM (1989) Signal sequences. Biochemistry 28, 923–930
Hageman, J, Baecke, C, Ebskamp, M, Pilon, M Smeekens, S & Weisbeek, PJ (1990) Protein import into and sorting inside the chloroplast are independent processes. Plant Cell 2: 479–494
Hall, PO & Rao, KK (1977) in: Encyclopedia of Plant Physiology 5: Pirson A and Zimmerman MH, Eds 206-215
Hall, DQ & Rao, KK (1987) Photosynthesis 4th Ed Edward Arnold Ltd, London
Hay, R, Bahni, P & Gasser, S (1984) How mitochondria import proteins. Biochim Biophys Acta 779: 65–87
Hirsch S, Michael E, Heemeyer F, Von Heijne G and Soli J (1994) A receptor component of the chloroplast protein translocation machinery. Science 266: 1989–1992
Homiak, L, Pilon, M, Van’t Hof, R & De Kruijff, B (1993) The secondary structure of the ferredoxin transit sequence is modulated by its interaction with negatively charged lipids. FEBS Lett 334: 241 — 246
Hovius, R, Lambrechts, H, Nicolay, K & De Kruijff, B (1990) Improved methods to isolate and subfractionate rat liver mitochondria. Lipid composition of the inner and outer membrane. BBA 1021: 217–226
Howard, KP & Prestigard, JH (1995) Membrane and solution conformations of monogalactosyldiacylglycerol using NMR/molecular modeling methods. J Am Chem Soc 117: 5031–5040
Keegstra, K (1989) Transport and routing of proteins into chloroplasts. Cell 56, 247–253
Kessler, F, Blobel, G, Patel, HA & Schnell, DJ (1994) Identification of two GTP-binding proteins in the chloroplast protein import machinery. Science 266: 1035–1039
Lancelin, J-M, Bally, I, Arland, GJ, Blackedge, M, Gans, P, Stein, M & Jacquot, J-P (1994) NMR structure of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution. FEBS Lett 350: 104–108
Müller, G & Zimmermann, R (1988) Import of honeybee prepromelittin into the endoplasmic reticulum: energy requirements for membrane insertion. EMBOJ 7: 639–648
Neupert, W & Lill, R (1992) Elsevier, Amsterdam. Membrane biogenesis and protein targeting
Olsen, LJ, Theg, SM, Selman, BR & Keegstra, K (1989) ATP is required for the binding of precursor proteins to chloroplasts. J Biol Chem 264: 6724–672
Perry, SE & Keegstra, K (1994) Envelope membrane proteins that interact with chloroplast precursor proteins. The plant cell 6: 93–105
Pilon, M, de Kruijff, B & Weisbeek, PJ (1992) New insights into the import mechanism of the ferredoxin precursor into chloroplasts. J Biol Chem 267: 2548—2556
Pilon, M, Rietveld, AG, Weisbeek, PJ & de Kruijff, B (1992) Secondary structure and folding of a functional chloroplast precursor protein. J Biol Chem 267: 19407—19413
Pilon, M, Weisbeek, PJ & De Kruijff, B (1992) Kinetic analysis of translocation into isolated chloroplasts of the purified ferredoxin precursor. FEBS Lett 302: 65–68
Pilon, M, Wienk, H, Sips, W, De Swaaf, ME, Talboom, F, Van ’t Hof, R, De Korte-Kool, G, Weisbeek, PJ & De Kruijff, B (1995) Functional domains of the ferredoxin transit sequence involved in chloroplast import. J Biol Chem 270: 3882–3893
Biochem Rapoport, TA (1992) Transport of proteins across the endoplasmic reticulum membrane. Science 258:931–936
Rietveld, AG, Koorengevel, MC & De Kruijff, B (1995) Non-bilayer lipids are required for efficient protein transport across the plasma membrane of Escherichia coli. EMBO J: in press
Robinson, G & Ellis, RJ (1984) Transport of proteins into chloroplasts. Partial purification of a chloroplast protease involved in the processing of imported precursor polypeptides. Eur J 142: 337–342
Roise, D & Schatz, G (1988) Mitochondrial presequences. J Biol Chem 263: 4509–4511
Sanders, SL & Schekman, R (1992) Polypeptide translocation across the endoplasmic reticulum membrane. J Biol Chem 267, 13791–13794
Schleyer, M, Schmidt, B & Neupert, W (1982) Requirement of a membrane potential for the posttranslational transfer of proteins into mitochondria. Eur J Biochem 125: 109–-116
Schnell, DJ, Blobel, G & Pain, D (1990) The chloroplast import receptor is an integral membrane protein of chloroplast envelope contact sites. J Cell Biol 111: 1825–1838
Schnell, DJ, Kessler, F & Blobel, G (1994) Isolation of components of the chloroplast protein import machinery. Science 266: 1007–1012
Seedorf, M & Soil, J (1995) Copper chloride, an inhibitor of protein import into chloroplasts. FEBS Lett 367: 19–22
Shipley, GG, Green, JP & Nichols, BW (1973) The phase behavior of monogalactosyl, digalactosyl and sulphoquinovosyl. Biochem Biophys Acta 311: 531—544
Smeekens, S, van Binsbergen, J & Weisbeek, PJ (1985) The plant ferredoxin precursor: nucleotide sequence of a full length cDNA done. Nucleic Acid Res 13: 3179–3194
Smeekens, S, van Steeg, H, Bauerle, C, Bettenbroek, H, Keegstra, K & Weisbeek, PJ (1987) Import into chloroplasts of a yeast mitochondrial protein directed by ferredoxin and plastocyanin transit peptides. Plant Mol Biol 9: 377–388
Sugiura, M (1992) The chloroplast genome. Plant Mol Biol 19: 149–168
Theg, SM, Bauerle, C, Olsen, LJ, Selman, BR & Keegstra, K (1989) Internal ATP is the only energy requirement for the translocation of precursor proteins across chloroplastic membranes. J BiolChem 264: 6730–6736
Umesono, K & Ozeki, H (1987) Chloroplast gene organization in plants. Trends Genet 3: 281—287
Van’t Hof, R, Demel, RA, Keegstra, K & De Kruijff, B (1991) Lipid-peptide interactions between fragments of the transit peptide of ribulose-l,5-bisphosphate carboxylase/oxygenase and chloroplast membrane lipids. FEBS Lett 291: 350–354
Van ’t Hof, R, Van Klompenburg, W, Pilon, M, Kozubek, A, De Korte-Kool, G, Demel, RA, Weisbeek, PJ & De Kruijff, B (1994) The transit sequence mediates the specific interaction of the precursor of ferredoxin with chloroplast envelope membrane lipids. J Biol Chem 268: 4037—4042
Van’t Hof, R & De Kruijff, B (1995) Transit sequence-dependent binding of the chloroplast precursor protein ferredoxin to lipid vesicles and its implications for membrane stability. FEBS Lett 356: 204— 206
Van’t Hof, R & De Kruijff, B (1995) Characterization of the import process of a transit peptide into chloroplasts. J Biol Chem (in press)
Von Heijne, G, Steppuhn, J & Herrmann, RG (1989) Domain structure of mitochondrial and chloroplast targeting peptides. Eur J Biochem 180: 535–545
Von Heijne, G & Nishikawa, K (1991) Chloroplast transit peptides. The perfect random coil?FEBS Lett 278: 1–3
Waegemann, K, Paulsen, H & Soil, J (1990) Translocation of proteins into isolated chloroplasts requires cytosolic factors to obtain import competence. FEBS Lett 261: 89–92
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1996 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
de Kruijff, B., Pilon, R., Van’t Hof, R., Demel, R. (1996). Lipid-protein interactions in chloroplast protein Import. In: Op den Kamp, J.A.F. (eds) Molecular Dynamics of Biomembranes. NATO ASI Series, vol 96. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-61126-1_10
Download citation
DOI: https://doi.org/10.1007/978-3-642-61126-1_10
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-64707-9
Online ISBN: 978-3-642-61126-1
eBook Packages: Springer Book Archive