Abstract
The functions of HSP90 chaperones in the protein-folding system and regulation of specific substrates affecting multiple signal pathways and cellular processes were considered. The triple role of HSP90 in stress was described: binding damaged proteins and directing them for refolding or degradation, regulation of the heat-shock gene induction, and alteration in the gene expression program. Based on the results of studies of the model species Arabidopsis thaliana, the role of HSP90 in growth maintenance and morphogenesis stability, developmental plasticity, and mechanisms of stress tolerance in plants was shown. A model for the interaction of the HSP90 functions under normal and stressful conditions is presented.
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