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Volumn 237, Issue 1, 1996, Pages 318-321

Potassium ions and the molecular-chaperone activity of DnaK

Author keywords

Adenosinetriphosphatase; DnaK; Molecular chaperone; Peptide ligand binding; Potassium

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; CHAPERONE; HEAT SHOCK PROTEIN 70; POTASSIUM ION;

EID: 0029933530     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0318n.x     Document Type: Article
Times cited : (45)

References (19)
  • 1
    • 0027954495 scopus 로고
    • Heat-shock proteins as molecular chaperones
    • Becker, J. & Craig, E. A. (1994) Heat-shock proteins as molecular chaperones, Eur. J. Biochem. 219, 11-23.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 11-23
    • Becker, J.1    Craig, E.A.2
  • 2
    • 0028268243 scopus 로고
    • Kinetics of molecular chaperone action
    • Schmid, D., Baici, A., Gehring, H. & 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
  • 3
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.-J. & 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
  • 4
    • 0026697941 scopus 로고
    • Precursor of mitochondrial aminotransferase synthesized in E.coli is complexed with heat shock protein DnaK
    • Schmid, D., Jaussi, R. & Christen, P. (1992) Precursor of mitochondrial aminotransferase synthesized in E.coli is complexed with heat shock protein DnaK, Eur. J. Biochem. 208, 699-704.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 699-704
    • Schmid, D.1    Jaussi, R.2    Christen, P.3
  • 5
    • 0021137114 scopus 로고
    • Purification and properties of the Escherichia coli dnak replication protein
    • Zylicz, M. & Georgopoulos, C. (1984) Purification and properties of the Escherichia coli dnak replication protein, J. Biol. Chem. 259, 8820-8825.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8820-8825
    • Zylicz, M.1    Georgopoulos, C.2
  • 6
    • 0023622594 scopus 로고
    • The grpE protein of Escherichia coli
    • Zylicz, M., Ang, D. & Georgopoulos, C. (1987) The grpE protein of Escherichia coli, J. Biol. Chem. 262, 17437-17442.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17437-17442
    • Zylicz, M.1    Ang, D.2    Georgopoulos, C.3
  • 7
    • 0026076490 scopus 로고
    • DnaK as a thermometer: Threonine-199 is site of autophosphorylation and is critical for ATPase activity
    • McCarthy, J. S. & Walker, G. C. (1991) DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity, Proc. Natl Acad. Sci. USA 88, 9513-9517.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 9513-9517
    • McCarthy, J.S.1    Walker, G.C.2
  • 8
    • 0027513927 scopus 로고
    • Nucleotide binding properties of bovine brain uncoating ATPase
    • Gao, B., Emoto, Y., Greene, L. & Eisenberg, E. (1993) Nucleotide binding properties of bovine brain uncoating ATPase, J. Biol. Chem. 268, 8507-8513.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8507-8513
    • Gao, B.1    Emoto, Y.2    Greene, L.3    Eisenberg, E.4
  • 9
    • 0028938819 scopus 로고
    • How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site
    • Wilbanks, S. M. & McKay, D. B. (1995) How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site, J. Biol. Chem. 270, 2251-2257.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2251-2257
    • Wilbanks, S.M.1    McKay, D.B.2
  • 10
    • 0028929052 scopus 로고
    • The DnaK chaperone system of Escherichia coli: Quaternary structures and interactions of the DnaK and GrpE components
    • Schönfeld, H.-J., Schmidt, D., Schröder, H. & 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
    • Schönfeld, H.-J.1    Schmidt, D.2    Schröder, H.3    Bukau, B.4
  • 11
    • 0028231720 scopus 로고
    • Characterization of nucleotide-free uncoating ATPase and its binding to ATP, ADP, and ATP analogues
    • Gao, B., Greene, L. & Eisenberg, E. (1994) Characterization of nucleotide-free uncoating ATPase and its binding to ATP, ADP, and ATP analogues, Biochemistry 33, 2048-2054.
    • (1994) Biochemistry , vol.33 , pp. 2048-2054
    • Gao, B.1    Greene, L.2    Eisenberg, E.3
  • 12
    • 85034935738 scopus 로고
    • Handbook of biochemistry and molecular biochemistry
    • CRC Press, Cleveland
    • Handbook of biochemistry and molecular biochemistry (1975) (Fasman, G. D., ed.) Nucleic acids vol. I, 3rd edn, p. 149, CRC Press, Cleveland.
    • (1975) Nucleic Acids Vol. I, 3rd Edn , vol.1 , pp. 149
    • Fasman, G.D.1
  • 13
    • 0027520036 scopus 로고
    • Bioluminometric assay of ADP and ATP at high ATP/ADP ratios: Assay of ADP after enzymatic removal of ATP
    • Schulz, V., Sussmann, I., Bokvist, K. & Tornheim, K. (1993) Bioluminometric assay of ADP and ATP at high ATP/ADP ratios: Assay of ADP after enzymatic removal of ATP, Anal. Biochem. 215, 302-304.
    • (1993) Anal. Biochem. , vol.215 , pp. 302-304
    • Schulz, V.1    Sussmann, I.2    Bokvist, K.3    Tornheim, K.4
  • 15
    • 0028897490 scopus 로고
    • How potassium affects the activity of the molecular chaperone Hsc70. I. Potassium is required for optimal ATPase activity
    • O'Brien, M. C. & McKay, D. B. (1995) How potassium affects the activity of the molecular chaperone Hsc70. I. Potassium is required for optimal ATPase activity, J. Biol. Chem. 270, 2247-2250.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2247-2250
    • O'Brien, M.C.1    McKay, D.B.2
  • 17
    • 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. & 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
  • 18
    • 0028980922 scopus 로고
    • Solution small angle X-ray scattering study of the molecular chaperone Hsc70 and its subfragments
    • Wilbanks, S. M., Chen, L., Tsuruta, H., Hodgson, K. O. & McKay, D. B. (1995) Solution small angle X-ray scattering study of the molecular chaperone Hsc70 and its subfragments, Biochemistry 34, 12095-12106.
    • (1995) Biochemistry , vol.34 , pp. 12095-12106
    • Wilbanks, S.M.1    Chen, L.2    Tsuruta, H.3    Hodgson, K.O.4    McKay, D.B.5
  • 19
    • 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., McCarthy, J. S., Virgallita, G., Milkereit, P., Reinstein, J. & 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    McCarthy, J.S.4    Virgallita, G.5    Milkereit, P.6    Reinstein, J.7    Bukau, B.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.