title: [Heat shock proteins of the hyperthermophilic archaea].
abstract: 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.
authors.affiliation: Institute for Biological Sciences, Jiangsu University, Zhenjiang 212013, China. hyc@ujs.edu.cn
authors.forename: Huayou
authors.initials: H
authors.lastname: Chen
authors.forename: Chunxia
authors.initials: C
authors.lastname: Zhang
authors.forename: Xiaoke
authors.initials: X
authors.lastname: Ma
authors.forename: Yi
authors.initials: Y
authors.lastname: Zhang
mesh_terms: 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
chemical_list: D019843:Archaeal Proteins; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; C112806:prefoldin