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Volumn 262, Issue 2, 1996, Pages 77-86

The '+70 pause': Hypothesis of a translational control of membrane protein assembly

Author keywords

Codon bias; Membrane protein assembly; mRNA translation; Protein targeting; Ribosome pausing

Indexed keywords

MEMBRANE PROTEIN; MESSENGER RNA;

EID: 0030595344     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0500     Document Type: Article
Times cited : (22)

References (47)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C. B. (1973). Principles that govern the folding of protein chains. Science, 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0016418420 scopus 로고
    • Intermediates in protein folding reactions and the mechanisms of protein folding
    • Baldwin, R. L. (1975). Intermediates in protein folding reactions and the mechanisms of protein folding. Annu. Rev. Biochem. 44, 453-475.
    • (1975) Annu. Rev. Biochem. , vol.44 , pp. 453-475
    • Baldwin, R.L.1
  • 3
    • 0025303147 scopus 로고
    • Interactions of hsp70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann, R. P., Mizzen, L. A. & Welch, W. J. (1990). Interactions of hsp70 with newly synthesized proteins: implications for protein folding and assembly. Science, 248, 850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.A.2    Welch, W.J.3
  • 4
    • 0020024572 scopus 로고
    • Codon selection in yeast
    • Bennetzen, J. L. & Hall, B. D. (1982). Codon selection in yeast. J. Biol. Chem. 257, 3026-3031.
    • (1982) J. Biol. Chem. , vol.257 , pp. 3026-3031
    • Bennetzen, J.L.1    Hall, B.D.2
  • 5
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes: Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma
    • Blobel, G. & Dobberstein, B. (1975). Transfer of proteins across membranes: presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol. 67, 835-851.
    • (1975) J. Cell Biol. , vol.67 , pp. 835-851
    • Blobel, G.1    Dobberstein, B.2
  • 6
    • 0014770988 scopus 로고
    • Controlled proteolysis of nascent polypeptides in rat liver cell fractions. I. Location of the polypeptides within ribosomes
    • Blobel, G. & Sabatini, D. D. (1970). Controlled proteolysis of nascent polypeptides in rat liver cell fractions. I. Location of the polypeptides within ribosomes. J. Cell Biol. 45, 130-145.
    • (1970) J. Cell Biol. , vol.45 , pp. 130-145
    • Blobel, G.1    Sabatini, D.D.2
  • 7
    • 0026459383 scopus 로고
    • Protein folding within the cell is influenced by controlled rates of polypeptide elongation
    • Crombie, T., Swaffield, J. C. & Brown, A. J. P. (1992). Protein folding within the cell is influenced by controlled rates of polypeptide elongation. J. Mol. Biol. 228, 7-12.
    • (1992) J. Mol. Biol. , vol.228 , pp. 7-12
    • Crombie, T.1    Swaffield, J.C.2    Brown, A.J.P.3
  • 9
    • 0019464222 scopus 로고
    • The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis
    • Engelman, D. M. & Steitz, T. A. (1981). The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis. Cell, 23, 411-422.
    • (1981) Cell , vol.23 , pp. 411-422
    • Engelman, D.M.1    Steitz, T.A.2
  • 10
    • 0028889120 scopus 로고
    • Contribution of cotranslational folding to the rate of formation of native protein structure
    • Fedorov, A. N. & Baldwin, T. O. (1995). Contribution of cotranslational folding to the rate of formation of native protein structure. Proc. Natl Acad. Sci. USA, 92, 1227-1231.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1227-1231
    • Fedorov, A.N.1    Baldwin, T.O.2
  • 11
    • 0026619867 scopus 로고
    • Folding on the ribosome of Escherichia coli tryptophan synthase beta subunit nascent chains probed with a conformation-dependent monoclonal antibody
    • Fedorov, A. N., Friguet, B., Djavadi-Ohaniance, L., Alakhov, Y. B. & Goldberg, M. E. (1992). Folding on the ribosome of Escherichia coli tryptophan synthase beta subunit nascent chains probed with a conformation-dependent monoclonal antibody. J. Mol. Biol. 228, 351-358.
    • (1992) J. Mol. Biol. , vol.228 , pp. 351-358
    • Fedorov, A.N.1    Friguet, B.2    Djavadi-Ohaniance, L.3    Alakhov, Y.B.4    Goldberg, M.E.5
  • 12
    • 0027184957 scopus 로고
    • Cotranslational assembly of some cytoskeletal proteins: Implications and prospects
    • Fulton, A. B. & L'Ecuyer, T. (1993). Cotranslational assembly of some cytoskeletal proteins: implications and prospects. J. Cell Sci. 105, 867-871.
    • (1993) J. Cell Sci. , vol.105 , pp. 867-871
    • Fulton, A.B.1    L'Ecuyer, T.2
  • 13
    • 0022384676 scopus 로고
    • The second translation of the genetic message: Protein folding and assembly
    • Goldberg, M. E. (1985). The second translation of the genetic message: protein folding and assembly. Trends Biochem. Sci. 10, 388-391.
    • (1985) Trends Biochem. Sci. , vol.10 , pp. 388-391
    • Goldberg, M.E.1
  • 14
    • 0020491327 scopus 로고
    • Codon usage in bacteria: Correlation with gene expressivity
    • Gouy, M. & Gautier, C. (1982). Codon usage in bacteria: correlation with gene expressivity. Nucl. Acids Res. 10, 7055-7074.
    • (1982) Nucl. Acids Res. , vol.10 , pp. 7055-7074
    • Gouy, M.1    Gautier, C.2
  • 15
    • 0022118360 scopus 로고
    • ACNUC - A portable retrieval system for nucleic acid sequence databases: Logical and physical designs and usage
    • Gouy, M., Gautier, C., Attimonelli, M., Lanave, C. & di Paola, G. (1985). ACNUC - a portable retrieval system for nucleic acid sequence databases: logical and physical designs and usage. Comp. Appl. Biosci. 1, 167-172.
    • (1985) Comp. Appl. Biosci. , vol.1 , pp. 167-172
    • Gouy, M.1    Gautier, C.2    Attimonelli, M.3    Lanave, C.4    Di Paola, G.5
  • 16
    • 0027218791 scopus 로고
    • Folding of the MS2 coat protein in Escherichia coli is modulated by translational pauses resulting from mRNA secondary structure and codon usage: A hypothesis
    • Guisez, Y., Robbens, J., Remaut, E. & Fiers, W. (1993). Folding of the MS2 coat protein in Escherichia coli is modulated by translational pauses resulting from mRNA secondary structure and codon usage: a hypothesis. J. Theoret. Biol. 162, 243-252.
    • (1993) J. Theoret. Biol. , vol.162 , pp. 243-252
    • Guisez, Y.1    Robbens, J.2    Remaut, E.3    Fiers, W.4
  • 17
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick, J. P. & Hartl, F.-U. (1993). Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62, 349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.-U.2
  • 18
    • 0022538848 scopus 로고
    • Determinants for protein translocation across mammalian endoplasmic reticulum. Membrane insertion of truncated and full-length prelysozyme molecules
    • Ibrahimi, I., Cutler, D., Steuber, D. & Bujard, H. (1986). Determinants for protein translocation across mammalian endoplasmic reticulum. Membrane insertion of truncated and full-length prelysozyme molecules. Eur. J. Biochem. 155, 571-576.
    • (1986) Eur. J. Biochem. , vol.155 , pp. 571-576
    • Ibrahimi, I.1    Cutler, D.2    Steuber, D.3    Bujard, H.4
  • 19
    • 0021958933 scopus 로고
    • Codon usage and tRNA content in unicellular and multicellular organisms
    • Ikemura, T. (1985). Codon usage and tRNA content in unicellular and multicellular organisms. Mol. Biol Evol. 2, 13-34.
    • (1985) Mol. Biol Evol. , vol.2 , pp. 13-34
    • Ikemura, T.1
  • 20
    • 0028243532 scopus 로고
    • Ubiquitin-assisted dissection of protein transport across membranes
    • Johnsson, N. & Varshavsky, A. (1994). Ubiquitin-assisted dissection of protein transport across membranes. EMBO J. 13, 2686-2698.
    • (1994) EMBO J. , vol.13 , pp. 2686-2698
    • Johnsson, N.1    Varshavsky, A.2
  • 21
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P. S. & Baldwin, R. L. (1990). Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59, 631-660.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 22
    • 0026047846 scopus 로고
    • Nonuniform size distribution of nascent globin peptides, evidence for pause localization sites, and a cotranslational protein-folding model
    • Krasheninnikov, I. A., Komar, A. A. & Adzhubei, I. A. (1991). Nonuniform size distribution of nascent globin peptides, evidence for pause localization sites, and a cotranslational protein-folding model. J. Protein Chem. 10, 445-453.
    • (1991) J. Protein Chem. , vol.10 , pp. 445-453
    • Krasheninnikov, I.A.1    Komar, A.A.2    Adzhubei, I.A.3
  • 23
    • 0020475449 scopus 로고
    • A simple method for displaying the hydrophobic character of a protein
    • Kyte, J. & Doolittle, R. F. (1982). A simple method for displaying the hydrophobic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 24
    • 0024363590 scopus 로고
    • The precursor of β-lactamase: Purification, properties and folding kinetics
    • Laminet, A. A. & Plückthun, A. (1989). The precursor of β-lactamase: purification, properties and folding kinetics. EMBO J. 8, 1469-1477.
    • (1989) EMBO J. , vol.8 , pp. 1469-1477
    • Laminet, A.A.1    Plückthun, A.2
  • 25
    • 0014202553 scopus 로고
    • Partial resistance of nascent polypeptide chains to proteolytic digestion due to ribosomal shielding
    • Malkin, L. I. & Rich, A. J. (1967). Partial resistance of nascent polypeptide chains to proteolytic digestion due to ribosomal shielding. J. Mol. Biol. 26, 329-346.
    • (1967) J. Mol. Biol. , vol.26 , pp. 329-346
    • Malkin, L.I.1    Rich, A.J.2
  • 26
    • 0023829903 scopus 로고
    • "DNA Strider": A "C" program for the fast analysis of DNA and protein sequences on the Apple Macintosh family of computers
    • Marck, C. (1988). "DNA Strider": a "C" program for the fast analysis of DNA and protein sequences on the Apple Macintosh family of computers. Nucl. Acids Res. 16, 1829-1836.
    • (1988) Nucl. Acids Res. , vol.16 , pp. 1829-1836
    • Marck, C.1
  • 27
    • 0024603438 scopus 로고
    • The yeast pyruvate kinase gene does not contain a string of non-preferred codons: Revised nucleotide sequence
    • McNally, T., Purvis, I. J., Fothergill-Gilmore, L. & Brown, A. J. P. (1989). The yeast pyruvate kinase gene does not contain a string of non-preferred codons: revised nucleotide sequence. FEBS Letters, 247, 312-316.
    • (1989) FEBS Letters , vol.247 , pp. 312-316
    • McNally, T.1    Purvis, I.J.2    Fothergill-Gilmore, L.3    Brown, A.J.P.4
  • 28
    • 0022588613 scopus 로고
    • Location of exit channel for nascent protein in 80 S ribosome
    • Milligan, R. A. & Unwin, P. N. (1986). Location of exit channel for nascent protein in 80 S ribosome. Nature, 319, 693-695.
    • (1986) Nature , vol.319 , pp. 693-695
    • Milligan, R.A.1    Unwin, P.N.2
  • 30
    • 0026649409 scopus 로고
    • The translation machinery and 70 kd heat shock protein cooperate in protein synthesis
    • Nelson, R. J., Ziegelhoffer, T., Nicolet, C., Werner-Washburne, M. & Craig, E. A. (1992). The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell, 71, 97-105.
    • (1992) Cell , vol.71 , pp. 97-105
    • Nelson, R.J.1    Ziegelhoffer, T.2    Nicolet, C.3    Werner-Washburne, M.4    Craig, E.A.5
  • 31
    • 0026049814 scopus 로고
    • Proper and improper folding of proteins in the cellular environment
    • Nilsson, B. & Anderson, S. (1991). Proper and improper folding of proteins in the cellular environment. Annu. Rev. Microbiol. 45, 607-635.
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 607-635
    • Nilsson, B.1    Anderson, S.2
  • 32
    • 0025305255 scopus 로고
    • Truncations of a secretory protein define minimum lengths required for binding to signal recognition particle and translocation across the endoplasmic reticulum membrane
    • Okun, M. M., Eskridge, E. M. & Shields, D. (1990). Truncations of a secretory protein define minimum lengths required for binding to signal recognition particle and translocation across the endoplasmic reticulum membrane. J. Biol. Chem. 265, 7478-7484.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7478-7484
    • Okun, M.M.1    Eskridge, E.M.2    Shields, D.3
  • 33
    • 0023882692 scopus 로고
    • Modulation of folding pathways of exported proteins by the leader sequence
    • Park, S., Liu, G., Topping, T. B., Cover, W. H. & Randall, L. L. (1988). Modulation of folding pathways of exported proteins by the leader sequence. Science, 239, 1033-1035.
    • (1988) Science , vol.239 , pp. 1033-1035
    • Park, S.1    Liu, G.2    Topping, T.B.3    Cover, W.H.4    Randall, L.L.5
  • 34
    • 0023659927 scopus 로고
    • The efficiency of folding of some proteins is increased by controlled rates of translation in vivo. An hypothesis
    • Purvis, I. J., Bettany, A. J. E., Santiago, T. C., Coggins, J. R., Duncan, K., Eason R. & Brown A. J. P. (1987). The efficiency of folding of some proteins is increased by controlled rates of translation in vivo. An hypothesis. J. Mol. Biol. 193, 413-417.
    • (1987) J. Mol. Biol. , vol.193 , pp. 413-417
    • Purvis, I.J.1    Bettany, A.J.E.2    Santiago, T.C.3    Coggins, J.R.4    Duncan, K.5    Eason, R.6    Brown, A.J.P.7
  • 35
    • 0017753965 scopus 로고
    • Synchronised transmembrane insertion and glycosylation of a nascent membrane protein
    • Rothman, J. E. & Lodish, H. F. (1977). Synchronised transmembrane insertion and glycosylation of a nascent membrane protein. Nature, 269, 775-780.
    • (1977) Nature , vol.269 , pp. 775-780
    • Rothman, J.E.1    Lodish, H.F.2
  • 36
    • 0025988205 scopus 로고
    • Synonymous codon usage in Saccharomyces cerevisiae
    • Sharp, P. M. & Cowe, E. (1991). Synonymous codon usage in Saccharomyces cerevisiae. Yeast, 7, 657-678.
    • (1991) Yeast , vol.7 , pp. 657-678
    • Sharp, P.M.1    Cowe, E.2
  • 37
    • 0023046211 scopus 로고
    • Codon usage in regulatory genes in Escherichia coli does not reflect selection for 'rare' codons
    • Sharp, P. M. & Li, W.-H. (1986). Codon usage in regulatory genes in Escherichia coli does not reflect selection for 'rare' codons. Nucl. Acids Res. 14, 7737-7749.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 7737-7749
    • Sharp, P.M.1    Li, W.-H.2
  • 38
    • 0023650543 scopus 로고
    • The codon adaptation index - A measure of directional synonymous codon usage bias, and its potential applications
    • Sharp, P. M. & Li, W.-H. (1987). The codon adaptation index - a measure of directional synonymous codon usage bias, and its potential applications. Nucl. Acids Res. 15, 1281-1295.
    • (1987) Nucl. Acids Res. , vol.15 , pp. 1281-1295
    • Sharp, P.M.1    Li, W.-H.2
  • 39
    • 0023737896 scopus 로고
    • Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum
    • Shaw, A. S., Rottier, P. J. M. & Rose, J. K. (1988). Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum. Proc. Natl Acad. Sci. USA, 85, 7592-7596.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 7592-7596
    • Shaw, A.S.1    Rottier, P.J.M.2    Rose, J.K.3
  • 40
    • 0024024901 scopus 로고
    • The affinity of signal recognition particle for presecretory proteins is dependent on nascent chain length
    • Siegel, V. & Walter, P. (1988). The affinity of signal recognition particle for presecretory proteins is dependent on nascent chain length. EMBO J. 7, 1769-1775.
    • (1988) EMBO J. , vol.7 , pp. 1769-1775
    • Siegel, V.1    Walter, P.2
  • 41
    • 0027058051 scopus 로고
    • Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum
    • Stirling, C. J., Rothblatt, J., Hosobuchi, M., Deshaies, R. & Schekman, R. (1992). Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol. Biol. Cell, 3, 129-142.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 129-142
    • Stirling, C.J.1    Rothblatt, J.2    Hosobuchi, M.3    Deshaies, R.4    Schekman, R.5
  • 42
    • 0017306279 scopus 로고
    • Evidence for variable rates of ribosome movement in Escherichia coli
    • Talkad, V., Schneider, E. & Kennell, D. (1976). Evidence for variable rates of ribosome movement in Escherichia coli. J. Mol. Biol. 104, 299-303.
    • (1976) J. Mol. Biol. , vol.104 , pp. 299-303
    • Talkad, V.1    Schneider, E.2    Kennell, D.3
  • 43
    • 0021764898 scopus 로고
    • Translation is a non-uniform process. Effect of tRNA availability on the rate of elongation of nascent polypeptide chains
    • Varenne, S., Buc, J., Lloubès, R. & Lazdunski, C. (1984). Translation is a non-uniform process. Effect of tRNA availability on the rate of elongation of nascent polypeptide chains. J. Mol. Biol. 180, 549-576.
    • (1984) J. Mol. Biol. , vol.180 , pp. 549-576
    • Varenne, S.1    Buc, J.2    Lloubès, R.3    Lazdunski, C.4
  • 44
    • 0021474773 scopus 로고
    • Protein translocation across the endoplasmic reticulum
    • Walter, P., Gilmore, R. & Blobel, G. (1984). Protein translocation across the endoplasmic reticulum. Cell, 38, 5-8.
    • (1984) Cell , vol.38 , pp. 5-8
    • Walter, P.1    Gilmore, R.2    Blobel, G.3
  • 45
    • 0027980239 scopus 로고
    • A protein complex required for signal-sequence-specific sorting and translocation
    • Wiedmann, B., Sakai, H., Davis, T. A. & Wiedmann, M. (1994). A protein complex required for signal-sequence-specific sorting and translocation. Nature, 370, 434-440.
    • (1994) Nature , vol.370 , pp. 434-440
    • Wiedmann, B.1    Sakai, H.2    Davis, T.A.3    Wiedmann, M.4
  • 46
    • 0024117032 scopus 로고
    • Ribosome pausing and stacking during translation of a eukaryotic mRNA
    • Wolin, S. L. & Walter, P. (1988). Ribosome pausing and stacking during translation of a eukaryotic mRNA. EMBO J. 7, 3559-3569.
    • (1988) EMBO J. , vol.7 , pp. 3559-3569
    • Wolin, S.L.1    Walter, P.2
  • 47
    • 0027189824 scopus 로고
    • Discrete nascent chain lengths are required for the insertion of presecretory proteins into microsomal membranes
    • Wolin, S. L. & Walter, P. (1993). Discrete nascent chain lengths are required for the insertion of presecretory proteins into microsomal membranes. J. Cell Biol. 121, 1211-1219.
    • (1993) J. Cell Biol. , vol.121 , pp. 1211-1219
    • Wolin, S.L.1    Walter, P.2


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