메뉴 건너뛰기




Volumn 162, Issue 3, 2002, Pages 1045-1053

Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; AMINO ACID; CHAPERONE; HEAT SHOCK PROTEIN 40; MUTANT PROTEIN; PROTEIN DNAJ; TRIPEPTIDE; DNAJ PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; HEAT SHOCK PROTEIN;

EID: 0036859957     PISSN: 00166731     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (88)

References (38)
  • 1
    • 0029879122 scopus 로고    scopus 로고
    • HLA-DR4 and HLA-DR10 motifs that carry susceptibility to rheumatoid arthritis bind 70-kD heat shock proteins
    • Auger, I., J. M. Escola, J. P. Gorvel and J. Roudier, 1996 HLA-DR4 and HLA-DR10 motifs that carry susceptibility to rheumatoid arthritis bind 70-kD heat shock proteins. Nat. Med. 2: 306-310.
    • (1996) Nat. Med. , vol.2 , pp. 306-310
    • Auger, I.1    Escola, J.M.2    Gorvel, J.P.3    Roudier, J.4
  • 2
    • 0034680778 scopus 로고    scopus 로고
    • NMR structure of the N-terminal J domain of murine polyomavirus T antigens: Implications for DnaJ-like domains and for mutations of T antigens
    • Berjanskii, M. V., M. I. Riley, A. Xie, V. Semenchenko, W. R. Folk et al., 2000 NMR structure of the N-terminal J domain of murine polyomavirus T antigens: Implications for DnaJ-like domains and for mutations of T antigens. J. Biol. Chem. 275: 36094-36103.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36094-36103
    • Berjanskii, M.V.1    Riley, M.I.2    Xie, A.3    Semenchenko, V.4    Folk, W.R.5
  • 3
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B., and A. L. Horwich, 1998 The Hsp70 and Hsp60 chaperone machines. Cell 92: 351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 4
    • 0026739395 scopus 로고
    • Regulation of eukaryotic hsp70 function by a dnaJ homolog
    • Cyr, D. M., X. Lu and M. G. Douglas, 1992 Regulation of eukaryotic hsp70 function by a dnaJ homolog. J. Biol. Chem. 267: 2092720931.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2092720931
    • Cyr, D.M.1    Lu, X.2    Douglas, M.G.3
  • 5
    • 0030929209 scopus 로고    scopus 로고
    • Structure-function analyses of the Ssc1p, Mdj1p, and Mge1p Saccharomyces cerevisiae mitochondrial proteins in Escherichia coli
    • Deloche, O., W. L. Kelley and C. Georgopoulos, 1997 Structure-function analyses of the Ssc1p, Mdj1p, and Mge1p Saccharomyces cerevisiae mitochondrial proteins in Escherichia coli. J. Bacteriol. 179: 6066-6075.
    • (1997) J. Bacteriol. , vol.179 , pp. 6066-6075
    • Deloche, O.1    Kelley, W.L.2    Georgopoulos, C.3
  • 7
    • 0035980016 scopus 로고    scopus 로고
    • Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor
    • Gassler, C. S., T. Wiederkehr, D. Brehmer, B. Bukau and M. P. Mayer, 2001 Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor. J. Biol. Chem. 276: 32538-32544.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32538-32544
    • Gassler, C.S.1    Wiederkehr, T.2    Brehmer, D.3    Bukau, B.4    Mayer, M.P.5
  • 8
    • 0035896599 scopus 로고    scopus 로고
    • DjlA is a third DnaK co-chaperone of Escherichia coli, and DjlA-mediated induction of colanic acid capsule requires DjlA-DnaK interaction
    • Genevaux, P., A. Wawrzynow, M. Zylicz, C. Georgopoulos and W. L. Kelley, 2001 DjlA is a third DnaK co-chaperone of Escherichia coli, and DjlA-mediated induction of colanic acid capsule requires DjlA-DnaK interaction. J. Biol. Chem. 276: 7906-7912.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7906-7912
    • Genevaux, P.1    Wawrzynow, A.2    Zylicz, M.3    Georgopoulos, C.4    Kelley, W.L.5
  • 9
    • 0032568541 scopus 로고    scopus 로고
    • Role of the J-domain in the cooperation of Hsp40 with Hsp70
    • Greene, M. K., K. Maskos and S. J. Landry, 1998 Role of the J-domain in the cooperation of Hsp40 with Hsp70. Proc. Natl. Acad. Sci. USA 95: 6108-6113.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6108-6113
    • Greene, M.K.1    Maskos, K.2    Landry, S.J.3
  • 10
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U., 1996 Molecular chaperones in cellular protein folding. Nature 381: 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 11
    • 0033670154 scopus 로고    scopus 로고
    • Analysis of the levels of conservation of the J domain among the various types of DnaJ-like proteins
    • Hennessy, F., M. E. Cheetham, H. W. Dirr and G. L. Blatch, 2000 Analysis of the levels of conservation of the J domain among the various types of DnaJ-like proteins. Cell Stress Chaperones 5: 347-358.
    • (2000) Cell Stress Chaperones , vol.5 , pp. 347-358
    • Hennessy, F.1    Cheetham, M.E.2    Dirr, H.W.3    Blatch, G.L.4
  • 12
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi, R., B. Krummel and R. K. Saiki, 1988 A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions. Nucleic Acids Res. 16: 7351-7367.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 13
    • 0029651968 scopus 로고
    • 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ (1-78)
    • 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ (1-78). Biochemistry 34: 5587-5596.
    • (1995) Biochemistry , vol.34 , pp. 5587-5596
    • Hill, R.B.1    Flanagan, J.M.2    Prestegard, J.H.3
  • 15
    • 15844372190 scopus 로고    scopus 로고
    • A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein
    • Karzai, A. W., and R. McMacken, 1996 A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein. J. Biol. Chem. 271: 11236-11246.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11236-11246
    • Karzai, A.W.1    McMacken, R.2
  • 16
    • 0032103439 scopus 로고    scopus 로고
    • The J-domain family and the recruitment of chaperone power
    • Kelley, W. L., 1998 The J-domain family and the recruitment of chaperone power. Trends Biochem. Sci. 23: 222-227.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 222-227
    • Kelley, W.L.1
  • 17
    • 0030935256 scopus 로고    scopus 로고
    • The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J-domain of the Escherichia coli DnaJ molecular chaperone
    • Kelley, W. L., and C. Georgopoulos, 1997 The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J-domain of the Escherichia coli DnaJ molecular chaperone. Proc. Natl. Acad. Sci. USA 94: 3679-3684.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3679-3684
    • Kelley, W.L.1    Georgopoulos, C.2
  • 18
    • 0035863048 scopus 로고    scopus 로고
    • Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen
    • Kim, H.-Y., B.-Y. Ahn and Y. Cho, 2001 Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen. EMBO J. 20: 295-304.
    • (2001) EMBO J. , vol.20 , pp. 295-304
    • Kim, H.-Y.1    Ahn, B.-Y.2    Cho, Y.3
  • 19
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., J. D. Roberts and R. A. Zakour, 1987 Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154: 367-383.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-383
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 20
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek, K., J. Marszalek, D. Ang, C. Georgopoulos and M. Zylicz, 1991 Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. USA 88: 2874-2878.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 22
    • 0030970268 scopus 로고    scopus 로고
    • Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP
    • Lyman, S. K., and R. Schekman, 1997 Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Cell 88: 85-96.
    • (1997) Cell , vol.88 , pp. 85-96
    • Lyman, S.K.1    Schekman, R.2
  • 23
    • 0032214832 scopus 로고    scopus 로고
    • J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences
    • Misselwitz, B., O. Staeck and T. A. Rapoport, 1998 J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences. Mol. Cell 2: 593-603.
    • (1998) Mol. Cell , vol.2 , pp. 593-603
    • Misselwitz, B.1    Staeck, O.2    Rapoport, T.A.3
  • 24
    • 0026545655 scopus 로고
    • Simian virus 40 mutants with amino-acid substitutions near the amino terminus of large T antigen
    • Peden, K. W., and J. M. Pipas, 1992 Simian virus 40 mutants with amino-acid substitutions near the amino terminus of large T antigen. Virus Genes 6: 107-118.
    • (1992) Virus Genes , vol.6 , pp. 107-118
    • Peden, K.W.1    Pipas, J.M.2
  • 25
    • 0030581175 scopus 로고    scopus 로고
    • Nmr structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone
    • Pellacchia, M., T. Szyperski, D. Wall, C. Georgopoulos and K. Wüthrich, 1996 Nmr structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. J. Mol. Biol. 260: 236-250.
    • (1996) J. Mol. Biol. , vol.260 , pp. 236-250
    • Pellacchia, M.1    Szyperski, T.2    Wall, D.3    Georgopoulos, C.4    Wüthrich, K.5
  • 26
    • 0030581148 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain
    • Qian, Y. Q., D. Patel, F.-U. Hartl and D. J. McColl, 1996 Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. J. Mol. Biol. 260: 224-235.
    • (1996) J. Mol. Biol. , vol.260 , pp. 224-235
    • Qian, Y.Q.1    Patel, D.2    Hartl, F.-U.3    McColl, D.J.4
  • 27
    • 0026410646 scopus 로고
    • A human homologue of the Escherichia coli DnaJ heat shock protein
    • Raabe, T., and J. L. Manley, 1991 A human homologue of the Escherichia coli DnaJ heat shock protein. Nucleic Acids Res. 19: 6645.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6645
    • Raabe, T.1    Manley, J.L.2
  • 28
    • 0029021905 scopus 로고
    • A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70's
    • Schlenstedt, G., S. Harris, B. Risse, R. Lill and P. A. Silver, 1995 A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70's. J. Cell Biol. 129: 979-988.
    • (1995) J. Cell Biol. , vol.129 , pp. 979-988
    • Schlenstedt, G.1    Harris, S.2    Risse, B.3    Lill, R.4    Silver, P.A.5
  • 29
    • 0026707466 scopus 로고
    • DnaK, DnaJ, and GrpE are required for flagellum synthesis in Escherichia coli
    • Shi, W., Y. Zhou, J. Wild, J. Adler and C. A. Gross, 1992 DnaK, DnaJ, and GrpE are required for flagellum synthesis in Escherichia coli. J. Bacteriol. 174: 6256-6263.
    • (1992) J. Bacteriol. , vol.174 , pp. 6256-6263
    • Shi, W.1    Zhou, Y.2    Wild, J.3    Adler, J.4    Gross, C.A.5
  • 30
  • 31
    • 0033929731 scopus 로고    scopus 로고
    • Species-specific elements in the large T-antigen J domain are required for cellular transformation and DNA replication by simian virus 40
    • Sullivan, C. S., J. D. Tremblay, S. W. Fewell, J. A. Lewis, J. L. Brodsky et al., 2000 Species-specific elements in the large T-antigen J domain are required for cellular transformation and DNA replication by simian virus 40. Mol. Cell. Biol. 20: 5749-5757.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5749-5757
    • Sullivan, C.S.1    Tremblay, J.D.2    Fewell, S.W.3    Lewis, J.A.4    Brodsky, J.L.5
  • 32
    • 0028151509 scopus 로고
    • The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system-DnaK, DnaJ, and GrpE
    • Szabo, A., T. Lancer, H. Schroder, J. Flanagan, B. Bukau et al., 1994 The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system-DnaK, DnaJ, and GrpE. Proc. Natl. Acad. Sci. USA 91: 10345-10349.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10345-10349
    • Szabo, A.1    Lancer, T.2    Schroder, H.3    Flanagan, J.4    Bukau, B.5
  • 33
    • 0027987996 scopus 로고
    • NMR structure determination of the Escherichia coli DnaJ molecular chaperone: Secondary structure and backbone fold of the N-terminal region (residues 2-108), containing the highly conserved J-domain
    • Szyperski, T., M. Pellacchia, D. Wall, C. Georgopoulos and K. Wüthrich, 1994 NMR structure determination of the Escherichia coli DnaJ molecular chaperone: Secondary structure and backbone fold of the N-terminal region (residues 2-108), containing the highly conserved J-domain. Proc. Natl. Acad. Sci. USA 91: 11343-11347.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11343-11347
    • Szyperski, T.1    Pellacchia, M.2    Wall, D.3    Georgopoulos, C.4    Wüthrich, K.5
  • 34
    • 0029871766 scopus 로고    scopus 로고
    • A conserved HPD sequence of the J-domain is necessary, for YDJ1 stimulation of hsp70 ATPase activity at a site distinct from substrate binding
    • Tsai, J., and M. G. Douglas, 1996 A conserved HPD sequence of the J-domain is necessary, for YDJ1 stimulation of hsp70 ATPase activity at a site distinct from substrate binding. J. Biol. Chem. 271: 4347-9354.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4347-9354
    • Tsai, J.1    Douglas, M.G.2
  • 35
    • 0029034167 scopus 로고
    • A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli
    • Ueguchi, C., T. Shiozawa, M. Kakeda, H. Yamada and T. Mizuno, 1995 A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli. J. Bacteriol. 177: 3894-3896.
    • (1995) J. Bacteriol. , vol.177 , pp. 3894-3896
    • Ueguchi, C.1    Shiozawa, T.2    Kakeda, M.3    Yamada, H.4    Mizuno, T.5
  • 36
    • 0028170215 scopus 로고
    • 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for λ replication
    • 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for λ replication. J. Biol. Chem. 269: 5446-5451.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5446-5451
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3
  • 37
    • 0026644011 scopus 로고
    • DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli
    • Wild, J., E. Altman, T. Yura and C. A. Gross, 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
  • 38
    • 0028921261 scopus 로고
    • The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates
    • Ziegelhoffer, T., P. Lopez-Buesa and E. A. Craig, 1995 The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J. Biol. Chem. 270: 10412-10419.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10412-10419
    • Ziegelhoffer, T.1    Lopez-Buesa, P.2    Craig, E.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.