[Heat shock proteins 90 kDa: diversity, structure, functions].
The review presents data on diversity, structure, functions and gene expression of the high conserved family of heat shock proteins 90 kDa (Hsp90). They are specialized molecular chaperones that fulfill the folding, maintenance of structural integrity and conformational regulation of a subset of proteins involved in important cellular processes, such as transduction of signals, cell cycle control etc. A composition and functioning of the Hsp90 chaperone machine are considered. Hsp90s play a significant role in growth and development of organisms carrying out conformational regulation of many regulatory proteins and protecting cells under stress. The review summarizes the results of investigations of different organisms, mainly animals and yeasts, with emphasis on the facts on Hsp90s in plants.
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Kozeko
D000818:Animals; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D010944:Plants; D017510:Protein Folding; D013312:Stress, Physiological / Q000502:physiology*; D013329:Structure-Activity Relationship; D015003:Yeasts
D018841:HSP90 Heat-Shock Proteins