HEAT SHOCK PROTEINS 90 kDa: DIVERSITY, STRUCTURE, FUNCTIONS
L. Ye. Kozeko
Institute of Botany, National Academy of Sciences of Ukraine, Kiev;
e-mail: kozeko@optima.com.ua
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.
Key words: heat shock protein Hsp90, cell protection, conformational regulation, structure, chaperone
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