Editorial: The HSP70 Molecular Chaperone Machines
نویسندگان
چکیده
منابع مشابه
Editorial: The HSP70 Molecular Chaperone Machines
The HSP70s belong to a small family of highly conserved ∼70 kDa enzymes that can use the energy of ATP-hydrolysis to modify the structure, and consequently the function, of specific native proteins, and to unfold, solubilize, and thereby reduce the cellular concentration of harmful misfolded proteins (Finka et al., 2016). Particular HSP70s are expressed constitutively in the cytosol of bacteria...
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This review is focused on the mechanisms by which ATP binding and hydrolysis drive chaperone machines assisting protein folding and unfolding. A survey of the key, general chaperone systems Hsp70 and Hsp90, and the unfoldase Hsp100 is followed by a focus on the Hsp60 chaperonin machine which is understood in most detail. Cryo-electron microscopy analysis of the E. coli Hsp60 GroEL reveals inter...
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ژورنال
عنوان ژورنال: Frontiers in Molecular Biosciences
سال: 2017
ISSN: 2296-889X
DOI: 10.3389/fmolb.2017.00001