Localization of calponin binding sites in the structure of 90 kDa heat shock protein (Hsp90)

FEBS Letters

Bogatcheva, Natalia V¹  Gusev, Nikolai B¹  Ma, YuShu¹  Urosev, Dunja¹ 

[1] Department of Biochemistry, School of Biology, Moscow State University, Moscow 119899, Russia

关键词: Heat shock protein;    Phosphorylation;    Casein kinase;    Calponin;    PVD;    polyvinylidene difluoride;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/S0014-5793(99)01056-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown