Heat shock protein (hsp90) interacts with smooth muscle calponin and affects calponin-binding to actin.
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.
Ma
Y
Y
Department of Biochemistry, School of Biology, Moscow State University, Moscow, Russia.
Bogatcheva
N V
NV
Gusev
N B
NB
D000199:Actins / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D008840:Microfilament Proteins; D009130:Muscle, Smooth / Q000378:metabolism; D011485:Protein Binding; D000096985:Calponins
D000199:Actins; D002135:Calcium-Binding Proteins; D018841:HSP90 Heat-Shock Proteins; D008840:Microfilament Proteins; D000096985:Calponins