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Vol 52(2018) N 5 p. 761-778; DOI 10.1134/S0026893318050138 Full Text

T.S. Tikhomirova1,2, O.V. Galzitskaya1*

Functionally Significant Amino Acid Motifs of Heat Shock Proteins: Structural and Bioinformatics Analyses of Hsp60/Hsp10 in Five Classes of Chordata

1Institute of Protein Research, Russian Academy of Sciences, Moscow oblast, Pushchino, 142290 Russia
2Institute for Biological Instrumentation, Russian Academy of Sciences, Moscow oblast, Pushchino, 142290 Russia

*ogalzit@vega.protres.ru
Received - 2017-11-27; Accepted - 2018-03-28

The Hsp60/Hsp10 chaperonin system is one of the most studied systems of cell emergency responses to stresses associated with changes in environmental conditions. In this regard, we have performed a bioinformatics analysis of 164 amino acid sequences of Hsp60 and 125 amino acid sequences of Hsp10 in five classes of chordata. This enabled uncovering the relationship between the identity of the amino acid composition of Hsp60/Hsp10 and the evolutionary distance between classes of chordata. In the course of the study of the chaperonin crystal structure, potentially significant amino acid motifs responsible for the oligomerization of Hsp60 and Hsp10 monomers and the association/dissociation of the Hsp60 and Hsp10 heterodimer have been identified. In addition, we have established that Hsp60 and Hsp10 can form amyloid fibrils due to structural features through the alternative using of the oligomerization sites of monomers as well as association/dissociation sites.

chaperonin, Hsp60/Hsp10, multiple alignment, chordata, oligomerization



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