Heat shock protein (hsp90) interacts with smooth muscle calponin and affects calponin-binding to actin

Yushu Ma, Natalia V. Bogatcheva, Nikolai B. Gusev

Research output: Contribution to journalArticle

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Interaction of smooth muscle calponin with 90 kDa heat shock protein (hsp90) was analyzed by means of native gel electrophoresis and affinity chromatography. Under conditions used, calponin and hsp90 form a complex with an apparent dissociation constant in the micromolar range. The major hsp90- binding site is located in the N-terminal (residues 7-144) part of calponin. Addition of calponin to actin-tropomyosin complex results in formation of actin bundles. Hsp90 partially prevents bundle formation without affecting the molar ratio calponin/actin in single actin filaments or actin bundles. At low ionic strength, calponin induces polymerization of G-actin. Hsp90 decreases calponin-induced polymerization of G-actin. It is supposed that hsp90 may be involved in the assembly of actin filaments. (C) 2000 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)300-310
Number of pages11
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Issue number2
StatePublished - Feb 9 2000



  • Actin
  • Calponin
  • Hsp90

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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