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Novel arrangement and comparative analysis of hsp90 family genes in three thermotolerant species of S tratiomyidae ( D iptera)
Author(s) -
Astakhova L. N.,
Zatsepina O. G.,
Przhiboro A. A.,
Evgen'ev M. B.,
Garbuz D. G.
Publication year - 2013
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1111/imb.12020
Subject(s) - biology , gene , gene family , heat shock protein , hsp70 , gene isoform , conserved sequence , genetics , sequence alignment , peptide sequence , hsp90 , promoter , genome , gene expression
The heat shock proteins belonging to the Hsp 90 family ( Hsp 83 in D iptera) play a crucial role in the protection of cells due to their chaperoning functions. We sequenced hsp90 genes from three species of the family S tratiomyidae ( D iptera) living in thermally different habitats and characterized by extraordinarily high thermotolerance. The sequence variation and structure of the hsp90 family genes were compared with previously described features of hsp70 copies isolated from the same species. Two functional hsp83 genes were found in the species studied, that are arranged in tandem orientation at least in one of them. This organization was not previously described. S tratiomyidae hsp83 genes share a high level of identity with hsp83 of D rosophila , and the deduced protein possesses five conserved amino acid sequence motifs characteristic of the Hsp 90 family as well as the C ‐terminus MEEVD sequence characteristic of the cytosolic isoform. A comparison of the hsp83 promoters of two S tratiomyidae species from thermally contrasting habitats demonstrated that while both species contain canonical heat shock elements in the same position, only one of the species contains functional GAF ‐binding elements. Our data indicate that in the same species, hsp83 family genes show a higher evolution rate than the hsp70 family.