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Volumn 25, Issue 1, 1997, Pages 53-64

Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition particle and trigger factor

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MEMBRANE PROTEIN; PROTEIN PRECURSOR; SECRETORY PROTEIN;

EID: 0030805752     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1997.4431808.x     Document Type: Article
Times cited : (150)

References (48)
  • 1
    • 0024966540 scopus 로고
    • Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle
    • Bernstein, H.D., Poritz, M.A., Strub, K., Hoben, P.J., Brenner, S., and Walter, P. (1989) Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle. Nature 340: 482-486.
    • (1989) Nature , vol.340 , pp. 482-486
    • Bernstein, H.D.1    Poritz, M.A.2    Strub, K.3    Hoben, P.J.4    Brenner, S.5    Walter, P.6
  • 2
    • 0027288333 scopus 로고
    • Functional substitution of the signal recognition particle 54-kDa subunit by its Escherichia coli homolog
    • Bernstein, H.D., Zopf, D., Freymann, D.M., and Walter, P. (1993) Functional substitution of the signal recognition particle 54-kDa subunit by its Escherichia coli homolog. Proc Natl Acad Sci USA 90: 5229-5233.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5229-5233
    • Bernstein, H.D.1    Zopf, D.2    Freymann, D.M.3    Walter, P.4
  • 3
    • 0024383748 scopus 로고
    • Mutations that improve export of maltose-binding protein in SecB - Cells of Escherichia coli
    • Collier, D.N., and Bassford, Jr, P.J. (1989) Mutations that improve export of maltose-binding protein in SecB - cells of Escherichia coli. J Bacteriol 171: 4640-4647.
    • (1989) J Bacteriol , vol.171 , pp. 4640-4647
    • Collier, D.N.1    Bassford Jr., P.J.2
  • 4
    • 0023387587 scopus 로고
    • Trigger factor: A soluble protein that folds pro-OmpA into a membrane-assembly competent form
    • Crooke, E., and Wickner, W. (1987) Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly competent form. Proc Natl Acad Sci USA 84: 5216-5220.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5216-5220
    • Crooke, E.1    Wickner, W.2
  • 5
    • 0030590843 scopus 로고    scopus 로고
    • Assembly of a cytoplasmic membrane protein in Escherichia coli is dependent on the signal recognition particle
    • De Gier, J.W.L., Mansournia, P., Valent, Q.A., Phillips, G.J., Luirink, J., and von Heijne, G. (1996) Assembly of a cytoplasmic membrane protein in Escherichia coli is dependent on the signal recognition particle. FEBS Lett 399: 307-309.
    • (1996) FEBS Lett , vol.399 , pp. 307-309
    • De Gier, J.W.L.1    Mansournia, P.2    Valent, Q.A.3    Phillips, G.J.4    Luirink, J.5    Von Heijne, G.6
  • 6
    • 0023187089 scopus 로고
    • Optimal posttranslational translocation of the precursor of PhoE protein across Escherichia coli membrane vesicles requires both ATP and the proton motive force
    • De Vrije, T., Tommassen, J., and de Kruijff, B. (1987) Optimal posttranslational translocation of the precursor of PhoE protein across Escherichia coli membrane vesicles requires both ATP and the proton motive force. Biochim Biophys Acta 900: 63-72.
    • (1987) Biochim Biophys Acta , vol.900 , pp. 63-72
    • De Vrije, T.1    Tommassen, J.2    De Kruijff, B.3
  • 7
    • 0027523180 scopus 로고
    • Titration of protein transport activity by incremental changes in signal peptide hydrophobicity
    • Doud, S.K., Chou, M.M., and Kendall, D.A. (1993) Titration of protein transport activity by incremental changes in signal peptide hydrophobicity. Biochemistry 32: 1251-1256.
    • (1993) Biochemistry , vol.32 , pp. 1251-1256
    • Doud, S.K.1    Chou, M.M.2    Kendall, D.A.3
  • 9
    • 0025003789 scopus 로고
    • Trigger factor depletion or overproduction causes defective cell division but does not block protein export
    • Guthrie, B., and Wickner, W. (1990) Trigger factor depletion or overproduction causes defective cell division but does not block protein export. J Bacteriol 172: 5555-5562.
    • (1990) J Bacteriol , vol.172 , pp. 5555-5562
    • Guthrie, B.1    Wickner, W.2
  • 10
    • 0025036708 scopus 로고
    • The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane
    • Hartl, F.-U., Lecker, S., Schiebel, E., Hendrick, J.P., and Wickner, W. (1990) The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. Cell 63: 269-279.
    • (1990) Cell , vol.63 , pp. 269-279
    • Hartl, F.-U.1    Lecker, S.2    Schiebel, E.3    Hendrick, J.P.4    Wickner, W.5
  • 11
    • 0028874760 scopus 로고
    • A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteins
    • Hauser, S., Bacher, G., Dobberstein, B., and Lütcke, H. (1995) A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteins. EMBO J 14: 5485-5493.
    • (1995) EMBO J , vol.14 , pp. 5485-5493
    • Hauser, S.1    Bacher, G.2    Dobberstein, B.3    Lütcke, H.4
  • 12
    • 0029913836 scopus 로고    scopus 로고
    • Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains
    • Hesterkamp, T., Hauser, S., Lütcke, H., and Bukau, B. (1996) Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proc Natl Acad Sci USA 93: 4437-4441.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4437-4441
    • Hesterkamp, T.1    Hauser, S.2    Lütcke, H.3    Bukau, B.4
  • 13
    • 0025762681 scopus 로고
    • Requirements for the membrane insertion of signal-anchor type proteins
    • High, S., Flint, N., and Dobberstein, B. (1991) Requirements for the membrane insertion of signal-anchor type proteins. J Cell Biol 113: 25-34.
    • (1991) J Cell Biol , vol.113 , pp. 25-34
    • High, S.1    Flint, N.2    Dobberstein, B.3
  • 14
    • 0030937725 scopus 로고    scopus 로고
    • Chloroplast SRP54 interacts specifically with a subset of thylakoid precursor proteins
    • High, S., Henry, R., Mould, R., Valent, Q.A., Meacock, S., Cline, K., Gray, J., and Luirink, J. (1997) Chloroplast SRP54 interacts specifically with a subset of thylakoid precursor proteins. J Biol Chem 272: 11622-11628.
    • (1997) J Biol Chem , vol.272 , pp. 11622-11628
    • High, S.1    Henry, R.2    Mould, R.3    Valent, Q.A.4    Meacock, S.5    Cline, K.6    Gray, J.7    Luirink, J.8
  • 15
    • 0025812217 scopus 로고
    • In vivo analysis of integration of membrane proteins in Escherichia coli
    • Ito, K., and Akiyama, Y. (1991) In vivo analysis of integration of membrane proteins in Escherichia coli. Mol Microbiol 5: 2243-2253.
    • (1991) Mol Microbiol , vol.5 , pp. 2243-2253
    • Ito, K.1    Akiyama, Y.2
  • 16
    • 0028849206 scopus 로고
    • Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins
    • Kandror, O., Sherman, M., Rhode, M., and Goldberg, A.L. (1995) Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins. EMBO J 14: 6021-6027.
    • (1995) EMBO J , vol.14 , pp. 6021-6027
    • Kandror, O.1    Sherman, M.2    Rhode, M.3    Goldberg, A.L.4
  • 17
    • 0021867206 scopus 로고
    • Evidence for specificity at an early step in protein export in Escherichia coli
    • Kumamoto, C.A., and Beckwith, J. (1985) Evidence for specificity at an early step in protein export in Escherichia coli. J Bacteriol 163: 267-274.
    • (1985) J Bacteriol , vol.163 , pp. 267-274
    • Kumamoto, C.A.1    Beckwith, J.2
  • 18
    • 0027189575 scopus 로고
    • Highly selective binding of nascent polypeptides by an Escherichia coli chaperone protein in vivo
    • Kumamoto, C.A., and Francetic, O. (1993) Highly selective binding of nascent polypeptides by an Escherichia coli chaperone protein in vivo. J Bacteriol 175: 2184-2188.
    • (1993) J Bacteriol , vol.175 , pp. 2184-2188
    • Kumamoto, C.A.1    Francetic, O.2
  • 19
    • 0024790857 scopus 로고
    • SecB stabilizes a translocation-competent state of purified prePhoE protein
    • Kusters, R., de Vrije, T., Breukink, E., and de Kruijff, B. (1989) SecB stabilizes a translocation-competent state of purified prePhoE protein. J Biol Chem 264: 20827-20830.
    • (1989) J Biol Chem , vol.264 , pp. 20827-20830
    • Kusters, R.1    De Vrije, T.2    Breukink, E.3    De Kruijff, B.4
  • 20
    • 0024449598 scopus 로고
    • Three pure chaperone proteins of Escherichia coli - SecB, trigger factor and GroEL - form soluble complexes with precursor proteins in vitro
    • Lecker, S., Lill, R., Ziegelhoffer, T., Georgopoulos, C., Bassford, P.J., Kumamoto, C.A., and Wickner, W. (1989) Three pure chaperone proteins of Escherichia coli - SecB, trigger factor and GroEL - form soluble complexes with precursor proteins in vitro. EMBO J 8: 2703-2709.
    • (1989) EMBO J , vol.8 , pp. 2703-2709
    • Lecker, S.1    Lill, R.2    Ziegelhoffer, T.3    Georgopoulos, C.4    Bassford, P.J.5    Kumamoto, C.A.6    Wickner, W.7
  • 21
    • 0028284220 scopus 로고
    • Mammalian and Escherichia coli signal recognition particles
    • Luirink, J., and Dobberstein, B. (1994) Mammalian and Escherichia coli signal recognition particles. Mol Microbiol 11: 9-13.
    • (1994) Mol Microbiol , vol.11 , pp. 9-13
    • Luirink, J.1    Dobberstein, B.2
  • 22
    • 0026616991 scopus 로고
    • Signal sequence recognition by an Escherichia coli ribonucleoprotein complex
    • Luirink, J., High, S., Wood, H., Giner, A., Tollervey, D., and Dobberstein, B. (1992) Signal sequence recognition by an Escherichia coli ribonucleoprotein complex. Nature 359: 741-743.
    • (1992) Nature , vol.359 , pp. 741-743
    • Luirink, J.1    High, S.2    Wood, H.3    Giner, A.4    Tollervey, D.5    Dobberstein, B.6
  • 24
    • 0028876220 scopus 로고
    • The functional integration of a polytopic membrane protein of Escherichia coli is dependent on the bacterial signal-recognition particle
    • MacFarlane, J., and Müller, M. (1995) The functional integration of a polytopic membrane protein of Escherichia coli is dependent on the bacterial signal-recognition particle. Eur J Biochem 233: 766-771.
    • (1995) Eur J Biochem , vol.233 , pp. 766-771
    • MacFarlane, J.1    Müller, M.2
  • 25
    • 0026769684 scopus 로고
    • Overproduction, purification and characterization of SecD and SecF, integral membrane components of the protein translocation machinery of Escherichia coli
    • Matsuyama, S., Fujita, Y., Sagara, K., and Mizushima, S. (1992) Overproduction, purification and characterization of SecD and SecF, integral membrane components of the protein translocation machinery of Escherichia coli. Biochim Biophys Acta 1122: 77-84.
    • (1992) Biochim Biophys Acta , vol.1122 , pp. 77-84
    • Matsuyama, S.1    Fujita, Y.2    Sagara, K.3    Mizushima, S.4
  • 26
    • 0019947629 scopus 로고
    • Secretory protein translocation across membranes - The role of 'docking protein'
    • Meyer, D.I., Krause, E., and Dobberstein, B. (1982) Secretory protein translocation across membranes - the role of 'docking protein'. Nature 297: 647-650.
    • (1982) Nature , vol.297 , pp. 647-650
    • Meyer, D.I.1    Krause, E.2    Dobberstein, B.3
  • 27
    • 0028158717 scopus 로고
    • Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor
    • Miller, J.D., Bernstein, H.D., and Walter, P. (1994) Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor. Nature 367: 657-659.
    • (1994) Nature , vol.367 , pp. 657-659
    • Miller, J.D.1    Bernstein, H.D.2    Walter, P.3
  • 28
    • 0027936633 scopus 로고
    • Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane
    • Mothes, W., Prehn, S., and Rapoport, T.A. (1994) Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane. EMBO J 13: 3973-3982.
    • (1994) EMBO J , vol.13 , pp. 3973-3982
    • Mothes, W.1    Prehn, S.2    Rapoport, T.A.3
  • 29
    • 0029952547 scopus 로고    scopus 로고
    • Signal sequences specify the targeting route to the endoplasmic reticulum membrane
    • Ng, D.T.W., Brown, J.D., and Walter, P. (1996) Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J Cell Biol 134: 269-278.
    • (1996) J Cell Biol , vol.134 , pp. 269-278
    • Ng, D.T.W.1    Brown, J.D.2    Walter, P.3
  • 30
    • 0028101487 scopus 로고
    • The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase
    • Nilsson, I., Whitley, P., and von Heijne, G. (1994) The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase. J Cell Biol 126: 1127-1132.
    • (1994) J Cell Biol , vol.126 , pp. 1127-1132
    • Nilsson, I.1    Whitley, P.2    Von Heijne, G.3
  • 31
    • 0028247158 scopus 로고
    • Requirement for conformational flexibility in the signal sequence of precursor protein
    • Nouwen, N., Tommassen, J., and de Kruijff, B. (1994) Requirement for conformational flexibility in the signal sequence of precursor protein. J Biol Chem 269: 16029-16033.
    • (1994) J Biol Chem , vol.269 , pp. 16029-16033
    • Nouwen, N.1    Tommassen, J.2    De Kruijff, B.3
  • 32
    • 0030018173 scopus 로고    scopus 로고
    • Substitution of 54 homologue (ffh) in Escherichia coli with the mammalian 54-kDa protein of signal-recognition particle
    • Patel, S., and Austen, B.M. (1996) Substitution of 54 homologue (ffh) in Escherichia coli with the mammalian 54-kDa protein of signal-recognition particle. Eur J Biochem 238: 760-768.
    • (1996) Eur J Biochem , vol.238 , pp. 760-768
    • Patel, S.1    Austen, B.M.2
  • 33
    • 0026794697 scopus 로고
    • The E. coli ffh gene is necessary for viability and efficient protein export
    • Phillips, G.J., and Silhavy, T.J. (1992) The E. coli ffh gene is necessary for viability and efficient protein export. Nature 359: 744-746.
    • (1992) Nature , vol.359 , pp. 744-746
    • Phillips, G.J.1    Silhavy, T.J.2
  • 34
    • 0025605808 scopus 로고
    • An E. coli ribonucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle
    • Poritz, M.A., Bernstein, H.D., Strub, K., Zopf, D., Wilhelm, H., and Walter, P. (1990) An E. coli ribonucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle. Science 250: 1111-1117.
    • (1990) Science , vol.250 , pp. 1111-1117
    • Poritz, M.A.1    Bernstein, H.D.2    Strub, K.3    Zopf, D.4    Wilhelm, H.5    Walter, P.6
  • 35
    • 0025009469 scopus 로고
    • E. coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle
    • Ribes, V., Römisch, K., Giner, A., Dobberstein, B., and Tollervey, D. (1990) E. coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle. Cell 63: 591-600.
    • (1990) Cell , vol.63 , pp. 591-600
    • Ribes, V.1    Römisch, K.2    Giner, A.3    Dobberstein, B.4    Tollervey, D.5
  • 36
    • 0024400708 scopus 로고
    • Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains
    • Römisch, K., Webb, J., Herz, J., Prehn, S., Frank, R., Vingron, M., and Dobberstein, B. (1989) Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains. Nature 340: 478-482.
    • (1989) Nature , vol.340 , pp. 478-482
    • Römisch, K.1    Webb, J.2    Herz, J.3    Prehn, S.4    Frank, R.5    Vingron, M.6    Dobberstein, B.7
  • 37
    • 0025012428 scopus 로고
    • The 54-kD protein of signal recognition particle contains a methionine-rich RNA binding domain
    • Römisch, K., Webb, J., Lingelbach, K., Gausepohl, H., and Dobberstein, B. (1990) The 54-kD protein of signal recognition particle contains a methionine-rich RNA binding domain. J Cell Biol 111: 1793-1802.
    • (1990) J Cell Biol , vol.111 , pp. 1793-1802
    • Römisch, K.1    Webb, J.2    Lingelbach, K.3    Gausepohl, H.4    Dobberstein, B.5
  • 38
    • 0027952825 scopus 로고
    • Transport of an export-defective protein by a highly hydrophobic signal peptide
    • Rusch, S.L., and Kendall, D.A. (1994) Transport of an export-defective protein by a highly hydrophobic signal peptide. J Biol Chem 269: 1243-1248.
    • (1994) J Biol Chem , vol.269 , pp. 1243-1248
    • Rusch, S.L.1    Kendall, D.A.2
  • 39
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G., and Dobberstein, B. (1996) Common principles of protein translocation across membranes. Science 271: 1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 40
    • 0031020515 scopus 로고    scopus 로고
    • FtsY, the prokaryotic signal recognition particle receptor homologue, is essential for biogenesis of membrane proteins
    • Seluanov, A., and Bibi, E. (1997) FtsY, the prokaryotic signal recognition particle receptor homologue, is essential for biogenesis of membrane proteins. J Biol Chem 272: 2053-2055.
    • (1997) J Biol Chem , vol.272 , pp. 2053-2055
    • Seluanov, A.1    Bibi, E.2
  • 41
    • 0028864461 scopus 로고
    • A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor
    • Stoller, G., Rücknagel, K.P., Nierhaus, K.H., Schmid, F.X., Fischer, G., and Rahfeld, J.U. (1995) A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J 14: 4939-4948.
    • (1995) EMBO J , vol.14 , pp. 4939-4948
    • Stoller, G.1    Rücknagel, K.P.2    Nierhaus, K.H.3    Schmid, F.X.4    Fischer, G.5    Rahfeld, J.U.6
  • 43
    • 0031472242 scopus 로고    scopus 로고
    • The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins
    • Ulbrandt, N.D., Newitt, J.A., and Bernstein, H.D. (1997) The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins. Cell 88: 187-196.
    • (1997) Cell , vol.88 , pp. 187-196
    • Ulbrandt, N.D.1    Newitt, J.A.2    Bernstein, H.D.3
  • 44
    • 0028799459 scopus 로고
    • Early events in preprotein recognition in E. coli: Interactions of SRP and trigger factor with nascent polypeptides
    • Valent, Q.A., Kendall, D.A., High, S., Kusters, R., Oudega, B., and Luirink, J. (1995) Early events in preprotein recognition in E. coli: interactions of SRP and trigger factor with nascent polypeptides. EMBO J 14: 5494-5505.
    • (1995) EMBO J , vol.14 , pp. 5494-5505
    • Valent, Q.A.1    Kendall, D.A.2    High, S.3    Kusters, R.4    Oudega, B.5    Luirink, J.6
  • 45
    • 0019822645 scopus 로고
    • 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
    • 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.
    • (1981) J Cell Biol , vol.91 , pp. 557-561
    • Walter, P.1    Blobel, G.2
  • 46
    • 0029112391 scopus 로고
    • NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase centre
    • Wang, S., Sakai, H., and Wiedmann, M. (1995) NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase centre. J Cell Biol 130: 519-528.
    • (1995) J Cell Biol , vol.130 , pp. 519-528
    • Wang, S.1    Sakai, H.2    Wiedmann, M.3
  • 47
    • 0025885002 scopus 로고
    • The enzymology of protein translocation across the Escherichia coli plasma membrane
    • Wickner, W., Driessen, A.J.M., and Hartl, F.U. (1991) The enzymology of protein translocation across the Escherichia coli plasma membrane. Annu Rev Biochem 60: 101-124.
    • (1991) Annu Rev Biochem , vol.60 , pp. 101-124
    • Wickner, W.1    Driessen, A.J.M.2    Hartl, F.U.3
  • 48
    • 0028365369 scopus 로고
    • From the elephant to E. coli: SRP-dependent protein targeting
    • Wolin, S.L. (1994) From the elephant to E. coli: SRP-dependent protein targeting. Cell 77: 787-790.
    • (1994) Cell , vol.77 , pp. 787-790
    • Wolin, S.L.1


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