[Heat shock proteins of the hyperthermophilic archaea].
As thermostable enzymes and organisms are much more needed, researches on heat shock proteins(HSPs) of hyperthermophilic archaea have drawn more concerns. HSPs from hyperthermophilic archaea are concise only with HSP60, sHSP, prefoldin and AAA+proteins, but without HSP100s, HSP90s, HSP70 (DnaK), HSP40 (DnaJ) and GrpE which are common in mesophilic or thermophilic archaea. Accordingly, studies on the structure, function and operation mechanism of these four groups are much more important and meaningful. This review focuses on the recent progress in the researchs on the structure, function, operation mechanism and cooperation of the HSPs from hyperthermophilic archaea. The problems and obfuscations in these HSPs are analyzed, and farther research direction and key points are put out.
Chen
Huayou
H
Institute for Biological Sciences, Jiangsu University, Zhenjiang 212013, China. hyc@ujs.edu.cn
Zhang
Chunxia
C
Ma
Xiaoke
X
Zhang
Yi
Y
D001105:Archaea / Q000145:classification / Q000378:metabolism*; D019843:Archaeal Proteins / Q000378:metabolism*; D018834:Chaperonin 60 / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism
D019843:Archaeal Proteins; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; C112806:prefoldin