Hsp70 chaperone machines

作者: Matthias P. Mayer , Dirk Brehmer , Claudia S. Gässler , Bernd Bukau

DOI: 10.1016/S0065-3233(01)59001-4

关键词:

摘要: Publisher Summary This chapter describes the molecular basis of Hsp70 chaperone machines. Particular emphasis is given to DnaK system Escherichia coli as it best understood system, and mechanistic differences between family members. The ubiquitous 70-kDa heat shock proteins (Hsp70s) assist an extraordinarily broad spectrum folding processes within entire life span proteins. These include newly synthesized misfolded proteins, prevention reversion protein aggregation, translocation organellar secretory across membranes, assembly disassembly oligomeric structures, control biological activity regulatory their co-chaperones constitute a complex network machines that utilized by cells in many ways. Despite considerable progress elucidation these machines, important aspects remain be solved. Furthermore, can expected more cellular will discovered depend on chaperones.

参考文章(218)
A. Szabo, R. Korszun, F. U. Hartl, J. Flanagan, A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates The EMBO Journal. ,vol. 15, pp. 408- 417 ,(1996) , 10.1002/J.1460-2075.1996.TB00371.X
C Ueguchi, T Shiozawa, M Kakeda, H Yamada, T Mizuno, A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli. Journal of Bacteriology. ,vol. 177, pp. 3894- 3896 ,(1995) , 10.1128/JB.177.13.3894-3896.1995
D Skowyra, S Wickner, The interplay of the GrpE heat shock protein and Mg2+ in RepA monomerization by DnaJ and DnaK. Journal of Biological Chemistry. ,vol. 268, pp. 25296- 25301 ,(1993) , 10.1016/S0021-9258(19)74391-9
B. Gao, Y. Emoto, L. Greene, E. Eisenberg, Nucleotide binding properties of bovine brain uncoating ATPase. Journal of Biological Chemistry. ,vol. 268, pp. 8507- 8513 ,(1993) , 10.1016/S0021-9258(18)52904-5
Bernd Bukau, Matthias P. Mayer, Hartwig Schröder, Stefan Rüdiger, Klaus Paal, Thomas Laufen, Multistep mechanism of substrate binding determines chaperone activity of Hsp70 Nature Structural & Molecular Biology. ,vol. 7, pp. 586- 593 ,(2000) , 10.1038/76819