Abstract
The movement of proteins from their site of synthesis in the cytosol to their final destination is fundamental for organelle and membrane biogenesis, secretion, and cellular organization. During the past 20 years, many advances have been made in our understanding of protein topogenesis—the process by which a protein achieves its topological distribution within a cell and, for an integral membrane protein, how it achieves its particular transmembrane topography (Blobel, 1980).
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References
Adelman, M. R., Sabatini, D. D., and Blobel, G., 1973, Ribosome—membrane interaction. Nondestructive disassembly of rat liver rough microsomes into ribosomal and membranous components, J. Cell Biol. 56:206–229.
Alloing, G., Trombe, M. C., and Claverys, J. P., 1990, The ami locus of the gram-positive bacterium Streptococcus pneumoniae is similar to binding protein-dependent transport operons of gram-negative bacteria, Mol. Microbiol. 4:633–644.
Blobel, G., 1980, Intracellular protein topogenesis, Proc. Natl. Acad. Sci. USA 77:1496–1500.
Blobel, G., and Dobberstein, B., 1975, Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components. J. Cell Biol. 67:852–862.
Blobel, G., and Sabatini, D. D., 1971, Ribosome-membrane interaction in eukaryotic cells, in: Biomembranes 2 (L. A. Manson, ed.), pp. 193–195, Plenum Press, New York.
Boulanger, P., and Letellier, L., 1988, Characterization of ion channels involved in the penetration of phage T4 DNA into Escherichia coli cells, J. Biol. Chem. 263:9767–9775.
Boulanger, P., and Letellier, L., 1992, Ion channels are likely to be involved in the two steps of phage T5 DNA penetration into Escherichia coli cells, J. Biol. Chem. 267:3168–3172.
Chang, C. N., Blobel, G., and Model, P., 1978, Detection of prokaryotic signal peptidase in an Escherichia coli membrane fraction: Endoproteolytic cleavage of nascent fl pre-coat protein, Proc. Natl., Acad. Sci. USA 75:361–365.
Connolly, T., and Gilmore, R., 1989, The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent Polypeptide, Cell 57:599–610.
Davidson, A. L., Shuman, H. A., and Nikaido, H., 1992, Mechanism of maltose transport in Escherichia coli: Transmembrane signaling by periplasmic binding proteins, Proc. Natl. Acad. Sci. USA 89:2360–2364.
Dobberstein, B., Blobel, G., and Chua, N. H., 1977, In vitro synthesis and processing of a putative precursor for the small subunit of ribulose-l,5-bisphosphate carboxylase of Chlamydomonas reinhardtii, Proc. Natl. Acad. Sci. USA 74:1082–1085.
Emr, S. D., and Silhavy, T. J., 1983, Importance of secondary structure in the signal sequence for protein secretion, Proc. Natl. Acad. Sci. USA 80:4599–4603.
Engelman, D. M., and Steitz, T. A., 1981, The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis, Cell 23:411–422.
Gilmore, R., Blobel, G., and Walter, P., 1982, Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle, J. Cell Biol. 95:463–469.
Gould, S. J., Keller, G.-A., and Subramani, S., 1988, Identification of peroxisomal targeting signals located at the carboxy terminus of four peroxisomal proteins, J. Cell Biol. 107:897–905.
Hann, B. C., and Walter, P., 1991, The signal recognition particle in S. cerevisiae, Cell 67:131–144.
Jiang, L. W., and Schindler, M., 1986, Chemical factors that influence nucleocytoplasmic transport: A fluorescence photobleaching study, J. Cell Biol. 102:853–858.
Kalderon, D., Roberts, B. L., Richardson, W. D., and Smith, A. E., 1984, A short amino acid sequence able to specify nuclear localization, Cell 39:499–509.
Kang, C. H., Shin, W. C., Yamagata, Y., Gokcen, S., Ames, G. F., and Kim, S. H., 1991, Crystal structure of the lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium at 2.7-A resolution, J. Biol. Chem. 266:23893–23899.
Kerppola, R. E., and Ames, G. F., 1992, Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease. Comparison with other members of the family, J. Biol. Chem. 267:2329–2336.
Lingappa, V. R., Katz, F. N., Lodish, H. F., and Blobel, G., 1978, A signal sequence for the insertion of a transmembrane glycoprotein. Similarities to the signals of secretory proteins in primary structure and function, J. Biol. Chem. 253:8667–8670.
Lubben, T. H., Bansberg, J., and Keegstra, K., 1987, Stop-transfer regions do not halt translocation of proteins into chloroplasts, Science 238:1112–1114.
Maccecchini, M. L., Rudin, Y, Blobel, G., and Schatz, G., 1979, Import of proteins into mitochondria: Precursor forms of the extramitochondrially made Fl-ATPase subunits in yeast, Proc. Natl. Acad. Sci. USA 76:343–347.
Miller, C., 1986, Ion Channel Reconstitution, Plenum Press, New York.
Morrison, D. A., Trombe, M. C., Hayden, M. K., Waszak, G. A., and Chen, J. D., 1984, Isolationof transformation-deficient Streptococcus pneumoniae mutants defective in control of competence, using insertion-duplication mutagenesis with the erythromycin resistance determinant of pAM beta 1, J. Bacteriol. 159:870–876.
Mueller, P., and Rudin, D. O., 1969, Bimolecular lipid membranes: Techniques of formation, study of electrical properties, and induction of ionic gating phenomena, in: Laboratory Techniques in Membrane Biophysics (H. Passow and R. Stampfil, eds.), pp. 141–156, Springer-Verlag, Berlin.
Mueller, P., Rudin, D. O., Ti Tien, H., and Wescott, W. C., 1962, Reconstitution of cell membrane structure in vitro and its transformation into an excitable system, Nature 194:979–980.
Nguyen, M., and Shore, G. C., 1987, Import of hybrid vesicular stomatitis G protein to the mitochondrial inner membrane, J. Biol. Chem. 262:3929–3931.
Paine, P. L., Moore, L. C., and Horowitz, S. B., 1975, Nuclear envelope permeability, Nature 254:109–114.
Redman, C. M., and Sabatini, D. D., 1966, Vectorial discharge of peptides released by puromycin from attached ribosomes, Proc. Natl. Acad. Sci. USA 56:608–615.
Redman, C. M., Siekevitz, P., and Palade, G. E., 1966, Synthesis and transfer of amylase in pigeon pancreatic microsomes, J. Biol. Chem. 241:1150–1158.
Roberts, R. B., Abelson, P. H., Cowie, D. B., Bolton, E. T., and Britten, R. J., 1963, Studies of Biosynthesis in Escherichia coli, Carnegie Institution of Washington, Washington, D.C.
Simon, S. M., and Blobel, G., 1991, A protein-conducting channel in the endoplasmic reticulum, Cell 65:1–10.
Simon, S. M., and Blobel, G., 1992, Signal peptides open protein-conducting channels in E. coli, Cell 69:677–684.
Simon, S. M., Blobel, G., and Zimmerberg, J., 1989, Large aqueous channels in membrane vesicles derived from the rough endoplasmic reticulum of canine pancreas or the plasma membrane of Escherichia coli, Proc. Natl. Acad. Sci. USA 86:6176–6180.
Simon, S. M., Peskin, C. S., and Oster, G. F., 1992, What drives the translocation of proteins, Proc. Natl. Acad. Sci. USA 89:3770–3774.
Singer, S. J., Maher, P. A., and Yaffe, M. P., 1987, On the translocation of proteins across membranes, Proc. Natl. Acad. Sci. USA 84:1015–1019.
Swinkels, B. W., Gould, S. J., Bodnar, A. G., Rachubinski, R. A., and Subramani, S., 1991, A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoA thiolase, EMBO J. 10:3255–3262.
Traut, R. R., and Monro, R. E., 1964, The puromycin reaction and its relation to protein synthesis, J. Mol. Biol. 10:63–72.
Trombe, M. C., Laneelle, G., and Sicard, A. M., 1984, Characterization of a Streptococcus pneumoniae mutant with altered electric transmembrane potential, J. Bacteriol. 158:1109–1114.
Vestweber, D., and Schatz, G., 1989, DNA-protein conjugates can enter mitochondria via the protein import pathway, Nature 338:170–172.
Von Heijne, G., and Blomberg, C., 1979, Transmembrane translocation of protein, Eur. J. Biochem. 97:175–181.
Walter, P., and Blobel, G., 1981, Translocation of proteins across the endoplasmic reticulum III. 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.
Walter, P., Ibrahimi, I., and Blobel, G., 1981, Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein, J. Cell Biol. 91:545–550.
Walter, P., Gilmore, R., and Blobel, G., 1984, Protein translocation across the endoplasmic reticulum, Cell 38:5–8.
Zimmerberg, J., Cohen, F. S., and Finkelstein, A., 1980, Micromolar Ca2+ stimulates fusion of lipid vesicles with planar bilayers containing a calcium-binding protein, Science 210:906–908.
Zimmermann, R., Zimmermann, M., Wiech, H., Schlenstedt, G., Müller, G., Morel, F., Klappa, P., Jung, C., and Cobet, W. W. E., 1990, Ribonucleoparticle-independent transport of proteins into mammalian microsomes, J. Bioenerg. Biomembr. 22:711–723.
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Simon, S.M., Blobel, G. (1993). Mechanisms of Translocation of Proteins across Membranes. In: Borgese, N., Harris, J.R. (eds) Endoplasmic Reticulum. Subcellular Biochemistry, vol 21. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2912-5_1
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DOI: https://doi.org/10.1007/978-1-4615-2912-5_1
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