作者: Matthias P. Mayer , Dirk Brehmer , Claudia S. Gässler , Bernd Bukau
DOI: 10.1016/S0065-3233(01)59001-4
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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.