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Volumn 27, Issue 2, 1998, Pages 469-476

Correlation between requirement for SecA during export and folding properties of precursor polypeptides

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CHAPERONE; OUTER MEMBRANE PROTEIN; PROTEIN PRECURSOR;

EID: 0031962436     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1998.00695.x     Document Type: Article
Times cited : (7)

References (36)
  • 1
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H.C., and Doly, J. (1979) A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res 7: 1513-1523.
    • (1979) Nucleic Acids Res , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 2
    • 0026687341 scopus 로고
    • In vitro studies on the folding characteristics of the Escherichia coli precursor protein PhoE
    • Breukink, E., Kusters, R., and de Kruijff, B. (1992) In vitro studies on the folding characteristics of the Escherichia coli precursor protein PhoE. Eur J Biochem 208: 419-425.
    • (1992) Eur J Biochem , vol.208 , pp. 419-425
    • Breukink, E.1    Kusters, R.2    De Kruijff, B.3
  • 3
    • 0026352441 scopus 로고
    • Characterization of the membrane-associated and soluble states of SecA protein from wild-type and SecA51 (ts) mutant strains of Escherichia coli
    • Cabelli, R.J., Dolan, K.M., Quan, L., and Oliver, D.B. (1991) Characterization of the membrane-associated and soluble states of SecA protein from wild-type and SecA51 (ts) mutant strains of Escherichia coli. J Biol Chem 266: 24420-24427.
    • (1991) J Biol Chem , vol.266 , pp. 24420-24427
    • Cabelli, R.J.1    Dolan, K.M.2    Quan, L.3    Oliver, D.B.4
  • 4
    • 0017129243 scopus 로고
    • Regulation of the regulatory gene for the arabinose pathway araC
    • Casadaban, M.J. (1976) Regulation of the regulatory gene for the arabinose pathway araC. J Mol Biol 104: 541-555.
    • (1976) J Mol Biol , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 5
    • 0028341055 scopus 로고
    • In vivo studies of the role of SecA during protein export in Escherichia coli
    • Chun, S-Y., and Randall, L.L. (1994) In vivo studies of the role of SecA during protein export in Escherichia coli. J Bacteriol 176: 4197-4203.
    • (1994) J Bacteriol , vol.176 , pp. 4197-4203
    • Chun, S.-Y.1    Randall, L.L.2
  • 6
    • 0027487182 scopus 로고
    • Folding of maltose-binding protein: Evidence for the identity of the rate-limiting step in vivo and in vitro
    • Chun, S-Y., Strobel, S., Bassford, Jr, P.J., and Randall, L.L. (1993) Folding of maltose-binding protein: evidence for the identity of the rate-limiting step in vivo and in vitro. J Biol Chem 268: 20855-20862.
    • (1993) J Biol Chem , vol.268 , pp. 20855-20862
    • Chun, S.-Y.1    Strobel, S.2    Bassford Jr., P.J.3    Randall, L.L.4
  • 7
    • 0024294402 scopus 로고
    • The anti-folding activity of SecB promotes the export of the Escherichia coli maltose-binding protein
    • Collier, D.N., Bankaitis, J.B., Weiss, P.J., Bassford, Jr, P.J. (1988) The anti-folding activity of SecB promotes the export of the Escherichia coli maltose-binding protein. Cell 53: 273-283.
    • (1988) Cell , vol.53 , pp. 273-283
    • Collier, D.N.1    Bankaitis, J.B.2    Weiss, P.J.3    Bassford Jr., P.J.4
  • 8
    • 0026577035 scopus 로고
    • Biogenesis of outer membrane protein PhoE of Escherichia coli. Evidence for multiple SecB-binding sites in the mature portion of the PhoE protein
    • de Cock, H., Overeem, W., and Tommassen, J. (1992) Biogenesis of outer membrane protein PhoE of Escherichia coli. Evidence for multiple SecB-binding sites in the mature portion of the PhoE protein. J Mol Biol 224: 369-379.
    • (1992) J Mol Biol , vol.224 , pp. 369-379
    • De Cock, H.1    Overeem, W.2    Tommassen, J.3
  • 9
    • 0023187089 scopus 로고
    • Optimal post-translational 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 post-translational 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
  • 11
    • 0025025813 scopus 로고
    • Electrochemical potential releases a membrane-bound secretion intermediate of maltose-binding protein in Escherichia coli
    • Geller, B.L. (1990) Electrochemical potential releases a membrane-bound secretion intermediate of maltose-binding protein in Escherichia coli. J Bacteriol 172: 4870-4876.
    • (1990) J Bacteriol , vol.172 , pp. 4870-4876
    • Geller, B.L.1
  • 12
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.-J., and Sambrook, J. (1992) Protein folding in the cell. Nature 355: 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 13
    • 0028142465 scopus 로고
    • Reconstitution of an efficient protein translocation machinery comprising SecA and the three membrane proteins, SecY, SecE and SecG (P12)*
    • Hanada, M., Nishiyama, K-I., Mizushima, S., and Tokuda, H. (1994) Reconstitution of an efficient protein translocation machinery comprising SecA and the three membrane proteins, SecY, SecE and SecG (P12)*. J Biol Chem 269: 23625-23631.
    • (1994) J Biol Chem , vol.269 , pp. 23625-23631
    • Hanada, M.1    Nishiyama, K.-I.2    Mizushima, S.3    Tokuda, H.4
  • 14
    • 0026025966 scopus 로고
    • A kinetic partitioning model of selective binding of non-native proteins by the bacterial chaperone SecB
    • Hardy, S.J.S., and Randall, L.L. (1991) A kinetic partitioning model of selective binding of non-native proteins by the bacterial chaperone SecB. Science 251: 439-433.
    • (1991) Science , vol.251 , pp. 439-1433
    • Hardy, S.J.S.1    Randall, L.L.2
  • 15
    • 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, W., 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, W.4    Wickner, W.5
  • 16
    • 0028270915 scopus 로고
    • Identification of a soluble SecA/SecB complex by means of a subfractionated cell-free export system
    • Hoffschulte, H.K., Drees, B., and Müller, M (1994) Identification of a soluble SecA/SecB complex by means of a subfractionated cell-free export system. J Biol Chem 269: 12833-12839.
    • (1994) J Biol Chem , vol.269 , pp. 12833-12839
    • Hoffschulte, H.K.1    Drees, B.2    Müller, M.3
  • 17
    • 0029075599 scopus 로고
    • Demonstration in vivo that interaction of maltose-binding protein with SecB is determined by a kinetic partitioning
    • Khisty, V.J., and Randall, L.L. (1995) Demonstration in vivo that interaction of maltose-binding protein with SecB is determined by a kinetic partitioning. J Bacteriol 177: 3277-3282.
    • (1995) J Bacteriol , vol.177 , pp. 3277-3282
    • Khisty, V.J.1    Randall, L.L.2
  • 18
    • 0343939593 scopus 로고
    • Escherichia coli SecB protein associates with exported protein precursors in vivo
    • Kumamoto, C.A. (1989) Escherichia coli SecB protein associates with exported protein precursors in vivo. Proc Natl Acad Sci USA 86: 5320-5324.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5320-5324
    • Kumamoto, C.A.1
  • 19
    • 0021867206 scopus 로고
    • Mutations in a new gene, secB, cause defective protein localization in Escherichia coli
    • Kumamoto, C.A., and Beckwith, J. (1985) Mutations in a new gene, secB, cause defective protein localization in Escherichia coli. J Bacteriol 163: 267-274.
    • (1985) J Bacteriol , vol.163 , pp. 267-274
    • Kumamoto, C.A.1    Beckwith, J.2
  • 20
    • 0027189575 scopus 로고
    • Highly selective binding of nascent polypeptides by an Escherichia coli chaperone
    • Kumamoto, C.A., and Francetic, O. (1993) Highly selective binding of nascent polypeptides by an Escherichia coli chaperone. J Bacteriol 175: 2184-2188.
    • (1993) J Bacteriol , vol.175 , pp. 2184-2188
    • Kumamoto, C.A.1    Francetic, O.2
  • 21
    • 0023710191 scopus 로고
    • Effects of Escherichia coli secB mutations on pre-maltose-binding protein conformation and export kinetics
    • Kumamoto, C.A., and Gannon, P.M. (1988) Effects of Escherichia coli secB mutations on pre-maltose-binding protein conformation and export kinetics. J Biol Chem 263: 11554-11558.
    • (1988) J Biol Chem , vol.263 , pp. 11554-11558
    • Kumamoto, C.A.1    Gannon, P.M.2
  • 22
    • 0025370548 scopus 로고
    • ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB protein
    • Lecker, S.H., Driessen, A.J.M., and Wickner, W. (1990) ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB protein. EMBO J 9: 2309-2314.
    • (1990) EMBO J , vol.9 , pp. 2309-2314
    • Lecker, S.H.1    Driessen, A.J.M.2    Wickner, W.3
  • 23
    • 0025019705 scopus 로고
    • The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins
    • Lill, R., Dowhan, W., and Wickner, W. (1990) The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins. Cell 60: 271-280.
    • (1990) Cell , vol.60 , pp. 271-280
    • Lill, R.1    Dowhan, W.2    Wickner, W.3
  • 26
    • 0001895079 scopus 로고
    • The mechanism of protein folding
    • Matthews, C.R. (1991) The mechanism of protein folding. Curr Opin Struct Biol 1: 28-35.
    • (1991) Curr Opin Struct Biol , vol.1 , pp. 28-35
    • Matthews, C.R.1
  • 27
    • 0023692599 scopus 로고
    • A peptide model of a protein folding intermediate
    • Oas, T.G., and Kim, P.S. (1988) A peptide model of a protein folding intermediate. Nature 336: 42-48.
    • (1988) Nature , vol.336 , pp. 42-48
    • Oas, T.G.1    Kim, P.S.2
  • 28
    • 0020171893 scopus 로고
    • Regulation of a membrane component required for protein secretion in Escherichia coli
    • Oliver, B.B., and Beckwith, J. (1982) Regulation of a membrane component required for protein secretion in Escherichia coli. Cell 30: 311-319.
    • (1982) Cell , vol.30 , pp. 311-319
    • Oliver, B.B.1    Beckwith, J.2
  • 29
    • 0017334421 scopus 로고
    • Synthesis of exported proteins by membrane-bound polysomes from Escherichia coli
    • Randall, L.L., and Hardy, S.J.S. (1977) Synthesis of exported proteins by membrane-bound polysomes from Escherichia coli. Eur J Biochem 75: 43-58.
    • (1977) Eur J Biochem , vol.75 , pp. 43-58
    • Randall, L.L.1    Hardy, S.J.S.2
  • 30
    • 0022553762 scopus 로고
    • Correlation between competence for export with lack of tertiary structure of the mature species: A study in vivo of maltose-binding protein in E. coli
    • Randall, L.L., and Hardy, S.J.S. (1986) Correlation between competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli. Cell 46: 921-928.
    • (1986) Cell , vol.46 , pp. 921-928
    • Randall, L.L.1    Hardy, S.J.S.2
  • 31
    • 0025315285 scopus 로고
    • No specific recognition of leader peptide by SecB, a chaperone involved in protein export
    • Randall, L.L., Topping, T.B., and Hardy, S.J.S. (1990) No specific recognition of leader peptide by SecB, a chaperone involved in protein export. Science 248: 860-863.
    • (1990) Science , vol.248 , pp. 860-863
    • Randall, L.L.1    Topping, T.B.2    Hardy, S.J.S.3
  • 32
    • 0022394361 scopus 로고
    • In vivo and in vitro synthesis of Escherichia coli maltose-binding protein under the regulatory control of the lac UV5 promoter-operator
    • Rasmussen, B.A., MacGregor, C.H., Ray, P.H., and Bassford, Jr, P.J. (1985) In vivo and in vitro synthesis of Escherichia coli maltose-binding protein under the regulatory control of the lac UV5 promoter-operator. J Bacteriol 164: 665-673.
    • (1985) J Bacteriol , vol.164 , pp. 665-673
    • Rasmussen, B.A.1    MacGregor, C.H.2    Ray, P.H.3    Bassford Jr., P.J.4
  • 33
    • 0026073817 scopus 로고
    • ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase
    • Schiebel, E., Driessen, A.J.M., Hartl, F.-U., and Wickner, W. (1991) ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase. Cell 64: 927-939.
    • (1991) Cell , vol.64 , pp. 927-939
    • Schiebel, E.1    Driessen, A.J.M.2    Hartl, F.-U.3    Wickner, W.4
  • 34
    • 0028214003 scopus 로고
    • Determination of the binding frame within a physiological ligand for the chaperone SecB
    • Topping, T.B., and Randall, L.L. (1994) Determination of the binding frame within a physiological ligand for the chaperone SecB. Protein Sci 3: 730-736.
    • (1994) Protein Sci , vol.3 , pp. 730-736
    • Topping, T.B.1    Randall, L.L.2
  • 35
    • 0024520431 scopus 로고
    • Factors influencing the in vitro translocation of Escherichia coli maltose-binding protein
    • Weiss, J.B., MacGregor, C.H., Collier, D.N., Fikes, J.D., Ray, P.H., and Bassford, Jr, P.J. (1989) Factors influencing the in vitro translocation of Escherichia coli maltose-binding protein. J Biol Chem 264: 3021-3027.
    • (1989) J Biol Chem , vol.264 , pp. 3021-3027
    • Weiss, J.B.1    MacGregor, C.H.2    Collier, D.N.3    Fikes, J.D.4    Ray, P.H.5    Bassford Jr., P.J.6
  • 36
    • 0026644011 scopus 로고
    • DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli
    • Wild, J., Altman, E., Yura, T., and Gross, C.A. (1992) DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli. Genes Dev 6: 1165-1172.
    • (1992) Genes Dev , vol.6 , pp. 1165-1172
    • Wild, J.1    Altman, E.2    Yura, T.3    Gross, C.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.