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Localization of calponin binding sites in the structure of 90 kDa heat shock protein (Hsp90)
Author(s) -
Bogatcheva Natalia V,
Ma YuShu,
Urosev Dunja,
Gusev Nikolai B
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01056-x
Subject(s) - casein kinase 2 , gene isoform , proteolysis , biochemistry , casein kinase 2, alpha 1 , peptide , hsp90 , calponin , heat shock protein , chemistry , phosphorylation , kinase , microbiology and biotechnology , protein kinase a , biology , casein kinase 1 , enzyme , mitogen activated protein kinase kinase , actin , gene
The structure of rabbit liver Hsp90 was reevaluated by limited trypsinolysis, N‐terminal sequencing and determination of the site that is phosphorylated by casein kinase II. Limited proteolysis results in formation of four groups of large peptides with M r in the range of 26–41 kDa. Peptides with M r 39–41 kDa were represented by large N‐terminal and central peptides starting at residue 283 of the α‐isoform of Hsp90. All sites phosphorylated by casein kinase II were located in the large 39–41 kDa peptides. Peptides with M r 26–27 kDa were represented by short N‐terminal and central peptides starting at Glu‐400 of the α‐isoform of Hsp90. The data of affinity chromatography and light scattering indicate that smooth muscle calponin interacts with Hsp90. The calponin binding sites are located in the large (37–41 kDa) N‐terminal and in a short (26–27 kDa) central peptide starting at Glu‐400 of the α‐isoform of Hsp90. Phosphorylation by casein kinase II up to 2 mol of phosphate per mol of Hsp90 does not affect interaction of Hsp90 with calponin.