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Volumn 20, Issue 9, 2012, Pages 1562-1573

Information encoded in Non-native states drives substrate-chaperone pairing

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHAPERONIN; PROTEIN DNAK; PROTEIN SECB;

EID: 84865704339     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.06.014     Document Type: Article
Times cited : (19)

References (34)
  • 3
    • 0024294402 scopus 로고
    • The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein
    • D.N. Collier, V.A. Bankaitis, J.B. Weiss, and P.J. Bassford Jr. The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein Cell 53 1988 273 283
    • (1988) Cell , vol.53 , pp. 273-283
    • Collier, D.N.1    Bankaitis, V.A.2    Weiss, J.B.3    Bassford, Jr.P.J.4
  • 5
    • 0032524646 scopus 로고    scopus 로고
    • D-peptide ligands for the co-chaperone DnaJ
    • B. Feifel, H.J. Schönfeld, and P. Christen D-peptide ligands for the co-chaperone DnaJ J. Biol. Chem. 273 1998 11999 12002
    • (1998) J. Biol. Chem. , vol.273 , pp. 11999-12002
    • Feifel, B.1    Schönfeld, H.J.2    Christen, P.3
  • 6
    • 0024614332 scopus 로고
    • The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export
    • P.M. Gannon, P. Li, and C.A. Kumamoto The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export J. Bacteriol. 171 1989 813 818
    • (1989) J. Bacteriol. , vol.171 , pp. 813-818
    • Gannon, P.M.1    Li, P.2    Kumamoto, C.A.3
  • 7
    • 2942650138 scopus 로고    scopus 로고
    • Fluorescence-aided molecule sorting: Analysis of structure and interactions by alternating-laser excitation of single molecules
    • A.N. Kapanidis, N.K. Lee, T.A. Laurence, S. Doose, E. Margeat, and S. Weiss Fluorescence-aided molecule sorting: analysis of structure and interactions by alternating-laser excitation of single molecules Proc. Natl. Acad. Sci. USA 101 2004 8936 8941
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8936-8941
    • Kapanidis, A.N.1    Lee, N.K.2    Laurence, T.A.3    Doose, S.4    Margeat, E.5    Weiss, S.6
  • 9
    • 0032574811 scopus 로고    scopus 로고
    • The sequences of small proteins are not extensively optimized for rapid folding by natural selection
    • D.E. Kim, H. Gu, and D. Baker The sequences of small proteins are not extensively optimized for rapid folding by natural selection Proc. Natl. Acad. Sci. USA 95 1998 4982 4986
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4982-4986
    • Kim, D.E.1    Gu, H.2    Baker, D.3
  • 11
    • 0024461843 scopus 로고
    • Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli
    • N. Kusukawa, T. Yura, C. Ueguchi, Y. Akiyama, and K. Ito Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli EMBO J. 8 1989 3517 3521
    • (1989) EMBO J. , vol.8 , pp. 3517-3521
    • Kusukawa, N.1    Yura, T.2    Ueguchi, C.3    Akiyama, Y.4    Ito, K.5
  • 12
    • 0024404941 scopus 로고
    • Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein
    • G. Liu, T.B. Topping, and L.L. Randall Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein Proc. Natl. Acad. Sci. USA 86 1989 9213 9217
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9213-9217
    • Liu, G.1    Topping, T.B.2    Randall, L.L.3
  • 14
    • 0026416043 scopus 로고
    • Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
    • J. Martin, T. Langer, R. Boteva, A. Schramel, A.L. Horwich, and F.U. Hartl Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate Nature 352 1991 36 42
    • (1991) Nature , vol.352 , pp. 36-42
    • Martin, J.1    Langer, T.2    Boteva, R.3    Schramel, A.4    Horwich, A.L.5    Hartl, F.U.6
  • 17
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • S. Rüdiger, L. Germeroth, J. Schneider-Mergener, and B. Bukau Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries EMBO J. 16 1997 1501 1507
    • (1997) EMBO J. , vol.16 , pp. 1501-1507
    • Rüdiger, S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 18
    • 0035283043 scopus 로고    scopus 로고
    • Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone
    • S. Rüdiger, J. Schneider-Mergener, and B. Bukau Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone EMBO J. 20 2001 1042 1050
    • (2001) EMBO J. , vol.20 , pp. 1042-1050
    • Rüdiger, S.1    Schneider-Mergener, J.2    Bukau, B.3
  • 19
    • 79952364237 scopus 로고    scopus 로고
    • Mechanics of Hsp70 chaperones enables differential interaction with client proteins
    • R. Schlecht, A.H. Erbse, B. Bukau, and M.P. Mayer Mechanics of Hsp70 chaperones enables differential interaction with client proteins Nat. Struct. Mol. Biol. 18 2011 345 351
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 345-351
    • Schlecht, R.1    Erbse, A.H.2    Bukau, B.3    Mayer, M.P.4
  • 21
    • 0031037687 scopus 로고    scopus 로고
    • Catalysis of protein folding by symmetric chaperone complexes
    • H. Sparrer, K. Rutkat, and J. Buchner Catalysis of protein folding by symmetric chaperone complexes Proc. Natl. Acad. Sci. USA 94 1997 1096 1100
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1096-1100
    • Sparrer, H.1    Rutkat, K.2    Buchner, J.3
  • 22
    • 0026763292 scopus 로고
    • Atomic interactions in protein-carbohydrate complexes. Tryptophan residues in the periplasmic maltodextrin receptor for active transport and chemotaxis
    • J.C. Spurlino, L.E. Rodseth, and F.A. Quiocho Atomic interactions in protein-carbohydrate complexes. Tryptophan residues in the periplasmic maltodextrin receptor for active transport and chemotaxis J. Mol. Biol. 226 1992 15 22
    • (1992) J. Mol. Biol. , vol.226 , pp. 15-22
    • Spurlino, J.C.1    Rodseth, L.E.2    Quiocho, F.A.3
  • 23
    • 0027486004 scopus 로고
    • Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coli
    • S.M. Strobel, J.G. Cannon, and P.J. Bassford Jr. Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coli J. Bacteriol. 175 1993 6988 6995
    • (1993) J. Bacteriol. , vol.175 , pp. 6988-6995
    • Strobel, S.M.1    Cannon, J.G.2    Bassford, Jr.P.J.3
  • 26
    • 0028214003 scopus 로고
    • Determination of the binding frame within a physiological ligand for the chaperone SecB
    • T.B. Topping, and L.L. Randall Determination of the binding frame within a physiological ligand for the chaperone SecB Protein Sci. 3 1994 730 736
    • (1994) Protein Sci. , vol.3 , pp. 730-736
    • Topping, T.B.1    Randall, L.L.2
  • 29
    • 0032514615 scopus 로고    scopus 로고
    • GroEL-GroES-mediated protein folding requires an intact central cavity
    • J.D. Wang, M.D. Michelitsch, and J.S. Weissman GroEL-GroES-mediated protein folding requires an intact central cavity Proc. Natl. Acad. Sci. USA 95 1998 12163 12168
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12163-12168
    • Wang, J.D.1    Michelitsch, M.D.2    Weissman, J.S.3
  • 30
    • 0025328710 scopus 로고
    • The folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro
    • J.B. Weiss, and P.J. Bassford Jr. The folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro J. Bacteriol. 172 1990 3023 3029
    • (1990) J. Bacteriol. , vol.172 , pp. 3023-3029
    • Weiss, J.B.1    Bassford, Jr.P.J.2
  • 31
    • 0026644011 scopus 로고
    • DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli
    • J. Wild, E. Altman, T. Yura, and C.A. Gross DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli Genes Dev. 6 1992 1165 1172
    • (1992) Genes Dev. , vol.6 , pp. 1165-1172
    • Wild, J.1    Altman, E.2    Yura, T.3    Gross, C.A.4
  • 32
    • 0029893301 scopus 로고    scopus 로고
    • Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli
    • J. Wild, P. Rossmeissl, W.A. Walter, and C.A. Gross Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli J. Bacteriol. 178 1996 3608 3613
    • (1996) J. Bacteriol. , vol.178 , pp. 3608-3613
    • Wild, J.1    Rossmeissl, P.2    Walter, W.A.3    Gross, C.A.4
  • 33
    • 70349470948 scopus 로고    scopus 로고
    • Structural and functional constraints in the evolution of protein families
    • C.L. Worth, S. Gong, and T.L. Blundell Structural and functional constraints in the evolution of protein families Nat. Rev. 10 2009 709 720
    • (2009) Nat. Rev. , vol.10 , pp. 709-720
    • Worth, C.L.1    Gong, S.2    Blundell, T.L.3
  • 34
    • 80051797261 scopus 로고    scopus 로고
    • Directed evolution of efficient secretion in the SRP-dependent export of TolB
    • Y.M. Zalucki, W.M. Shafer, and M.P. Jennings Directed evolution of efficient secretion in the SRP-dependent export of TolB Biochim. Biophys. Acta 1808 2011 2544 2550
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2544-2550
    • Zalucki, Y.M.1    Shafer, W.M.2    Jennings, M.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.