메뉴 건너뛰기




Volumn 15, Issue 3, 1996, Pages 607-617

A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor σ32

Author keywords

Heat shock protein; Heat shock response; Hsp70; Protein folding; Sigma factor

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN; TRANSCRIPTION FACTOR;

EID: 0030044799     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00393.x     Document Type: Article
Times cited : (246)

References (43)
  • 2
    • 0028382510 scopus 로고
    • A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE
    • Buchberger, A., Schröder, H., Büttner, M., Valencia, A. and Bukau, B. (1994a) A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Nature Struct. Biol., 1, 95-101.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 95-101
    • Buchberger, A.1    Schröder, H.2    Büttner, M.3    Valencia, A.4    Bukau, B.5
  • 3
    • 0028297010 scopus 로고
    • The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171
    • Buchberger, A., Valencia, A., McMacken, R., Sander, C. and Bukau, B. (1994b) The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171. EMBO J., 13, 1687-1695.
    • (1994) EMBO J. , vol.13 , pp. 1687-1695
    • Buchberger, A.1    Valencia, A.2    McMacken, R.3    Sander, C.4    Bukau, B.5
  • 4
    • 0029037015 scopus 로고
    • Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication
    • Buchberger, A., Theyssen, H., Schröder, H., McCarry, J.S., Virgallita, G., Milkereit, P., Reinstein, J. and Bukau, B. (1995) Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication. J. Biol. Chem., 270, 16903-16910.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16903-16910
    • Buchberger, A.1    Theyssen, H.2    Schröder, H.3    McCarry, J.S.4    Virgallita, G.5    Milkereit, P.6    Reinstein, J.7    Bukau, B.8
  • 6
    • 0027319272 scopus 로고
    • Regulation of the E. coli heat shock response
    • Bukau, B. (1993) Regulation of the E. coli heat shock response. Mol. Microbiol., 9, 671-680.
    • (1993) Mol. Microbiol. , vol.9 , pp. 671-680
    • Bukau, B.1
  • 7
    • 0025967766 scopus 로고
    • Is hsp70 the cellular thermometer?
    • Craig, E.A. and Gross, C.A. (1991) Is hsp70 the cellular thermometer? Trends Biochem. Sci., 16, 135-140.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 135-140
    • Craig, E.A.1    Gross, C.A.2
  • 9
    • 0002377439 scopus 로고
    • Properties of the Escherichia coli heat shock proteins and their role in bacteriophage λ growth
    • Morimoto, R. Tissières, A. and Georgopoulos, C. (eds), Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY
    • Georgopoulos, C., Ang, D., Liberek, K. and Zylicz, M. (1990) Properties of the Escherichia coli heat shock proteins and their role in bacteriophage λ growth. In Morimoto, R. Tissières, A. and Georgopoulos, C. (eds), Stress Proteins in Biology and Medicine. Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY, pp. 191-222.
    • (1990) Stress Proteins in Biology and Medicine , pp. 191-222
    • Georgopoulos, C.1    Ang, D.2    Liberek, K.3    Zylicz, M.4
  • 10
    • 0000757557 scopus 로고
    • Properties of the heat shock proteins of Escherichia coli and the autoregulation of the heat shock response
    • Morimoto, R.I. Tissières, A. and Georgopoulos, C. (eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Georgopoulos, C., Liberek, K., Zylicz, M. and Ang, D. (1994) Properties of the heat shock proteins of Escherichia coli and the autoregulation of the heat shock response. In Morimoto, R.I. Tissières, A. and Georgopoulos, C. (eds), The Biology of Heat Shock Proteins and Molecular Chaperones. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 209-250.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 209-250
    • Georgopoulos, C.1    Liberek, K.2    Zylicz, M.3    Ang, D.4
  • 11
    • 0000217854 scopus 로고
    • The function and regulation of heat shock proteins in Escherichia coli
    • Morimoto, R. Tissières, A. and Georgopoulos, C. (eds). Cold Sprine Harbor Laboratory Press, Cold Spring Harbor, NY
    • Gross, C.A., Straus, D.B. and Erickson, J.W. (1990) The function and regulation of heat shock proteins in Escherichia coli. In Morimoto, R. Tissières, A. and Georgopoulos, C. (eds). Stress Proteins in Biology and Medicine. Cold Sprine Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 167-190.
    • (1990) Stress Proteins in Biology and Medicine , pp. 167-190
    • Gross, C.A.1    Straus, D.B.2    Erickson, J.W.3
  • 12
    • 0023322682 scopus 로고
    • Sigma 32 synthesis can regulate the synthesis of heat shock proteins in Escherichia coli
    • Grossman, A.D., Straus, D.B., Walter, W.A. and Gross, C.A. (1987) Sigma 32 synthesis can regulate the synthesis of heat shock proteins in Escherichia coli. Genes Dev., 1, 179-84.
    • (1987) Genes Dev. , vol.1 , pp. 179-184
    • Grossman, A.D.1    Straus, D.B.2    Walter, W.A.3    Gross, C.A.4
  • 13
    • 0028584378 scopus 로고
    • ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain
    • Ha, J.-H. and McKay, D.B. (1994) ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain. Biochemistry, 33, 14625-14635.
    • (1994) Biochemistry , vol.33 , pp. 14625-14635
    • Ha, J.-H.1    McKay, D.B.2
  • 14
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E. and Lane, D. (1988) Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 15
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick, J.P. and 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
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0026595140 scopus 로고
    • Different conformations for the same polypeptide bound to chaperones DnaK and GroEL
    • Landry, S.J., Jordan, R., McMacken, R. and Gierasch, L.M. (1992) Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature, 355, 455-457.
    • (1992) Nature , vol.355 , pp. 455-457
    • Landry, S.J.1    Jordan, R.2    McMacken, R.3    Gierasch, L.M.4
  • 20
    • 0027504094 scopus 로고
    • Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins
    • Liberek, K. and Georgopoulos, C. (1993) Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins. Proc. Natl Acad. Sci. USA, 90, 11019-11023.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11019-11023
    • Liberek, K.1    Georgopoulos, C.2
  • 21
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek, K., Marszalek, J., Ang, D., Georgopoulos, C. and Zylicz, M. (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
  • 24
    • 0018780589 scopus 로고
    • Purification and properties of the σ subunit of Escherichia coli DNA-dependent RNA polymerase
    • Lowe, P.A., Hager, D.A. and Burgess, R.R. (1978) Purification and properties of the σ subunit of Escherichia coli DNA-dependent RNA polymerase. Biochemistry, 18, 1344-1352.
    • (1978) Biochemistry , vol.18 , pp. 1344-1352
    • Lowe, P.A.1    Hager, D.A.2    Burgess, R.R.3
  • 25
    • 0027916175 scopus 로고
    • Biospecific interaction analysis using biosensor technology
    • Malmquist, M. (1993) Biospecific interaction analysis using biosensor technology. Nature, 361, 186-187.
    • (1993) Nature , vol.361 , pp. 186-187
    • Malmquist, M.1
  • 26
    • 0029013908 scopus 로고
    • The role of ATP in the functional cycle of the DnaK chaperone system
    • McCarty, J.S., Buchberger, A., Reinstein, J. and Bukau, B. (1995) The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol., 249, 126-137.
    • (1995) J. Mol. Biol. , vol.249 , pp. 126-137
    • McCarty, J.S.1    Buchberger, A.2    Reinstein, J.3    Bukau, B.4
  • 30
    • 0028268243 scopus 로고
    • Kinetics of molecular chaperone action
    • Schmid, D., Baici, A., Gehring, H. and Christen, P. (1994) Kinetics of molecular chaperone action. Science, 263, 971-973.
    • (1994) Science , vol.263 , pp. 971-973
    • Schmid, D.1    Baici, A.2    Gehring, H.3    Christen, P.4
  • 31
    • 0028929052 scopus 로고
    • The DnaK chaperone system of Escherichia coli: Quaternary structures and interactions of the DnaK and GrpE components
    • Schonfeld, H.-J., Schmidt D., Schröder, H. and Bukau, B. (1995) The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components. J. Biol. Chem., 270, 2183-2189.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2183-2189
    • Schonfeld, H.-J.1    Schmidt, D.2    Schröder, H.3    Bukau, B.4
  • 32
    • 0027427986 scopus 로고
    • DnaK, DnaJ, GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
    • Schröder, H., Langer, T., Hartl, F.-U. and Bukau, B. (1993) DnaK, DnaJ, GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J., 12, 4137-4144.
    • (1993) EMBO J. , vol.12 , pp. 4137-4144
    • Schröder, H.1    Langer, T.2    Hartl, F.-U.3    Bukau, B.4
  • 34
    • 0024854864 scopus 로고
    • 32 is reduced under conditions of excess heat shock protein production in Escherichia coli
    • 32 is reduced under conditions of excess heat shock protein production in Escherichia coli. Genes Dev., 3, 2003-2010.
    • (1989) Genes Dev. , vol.3 , pp. 2003-2010
    • Straus, D.B.1    Walter, W.A.2    Gross, C.A.3
  • 36
    • 0028151509 scopus 로고
    • Chaperoned protein folding by the E. coli Hsp70 system DnaK, DnaJ and GrpE
    • Szabo, A., Langer, T., Schröder, H., Bukau, B. and Hartl, F.U. (1994) Chaperoned protein folding by the E. 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    Langer, T.2    Schröder, H.3    Bukau, B.4    Hartl, F.U.5
  • 39
    • 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
  • 40
    • 0028930540 scopus 로고
    • The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone
    • Wall, D., Zylicz, M. and Georgopoulos, C. (1995) The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone. J. Biol. Chem., 270, 2139-2144.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2139-2144
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3
  • 41
    • 0029094250 scopus 로고
    • Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates
    • Wawrzynów, A. and Zylicz, M. (1995) Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates. J. Biol. Chem., 270, 19300-19306.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19300-19306
    • Wawrzynów, A.1    Zylicz, M.2
  • 42
    • 0027385183 scopus 로고
    • Regulation of the heat-shock response in bacteria
    • Yura, T., Nagai, H. and Mori, H. (1993) Regulation of the heat-shock response in bacteria. Annu. Rev. Microbiol., 47, 321-350.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 321-350
    • Yura, T.1    Nagai, H.2    Mori, H.3
  • 43
    • 0021880465 scopus 로고
    • Purification and properties of the DnaJ replication protein of Escherichia coli
    • Zylicz, M., Yamamoto, T., McKittrick, N., Sell, S. and Georgopoulos, C. (1985) Purification and properties of the DnaJ replication protein of Escherichia coli. J. Biol Chem., 260, 7591-7598.
    • (1985) J. Biol Chem. , vol.260 , pp. 7591-7598
    • Zylicz, M.1    Yamamoto, T.2    McKittrick, N.3    Sell, S.4    Georgopoulos, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.