title: Correlation between calponin and myosin subfragment 1 binding to F-actin and ATPase inhibition.
abstract: Calponin is a thin-filament-associated protein that has been implicated in the regulation of smooth-muscle contractility. It binds to F-actin and inhibits the MgATPase activity of actomyosin. In the present work we have examined the effect of recombinant chicken gizzard alpha-calponin (R alpha CaP) on the binding of rabbit skeletal-muscle myosin subfragment 1 (S1) to F-actin and on the inhibition of its actin-activated MgATPase. We have found that binding of one R alpha CaP molecule to every three to four actin monomers is sufficient for maximal inhibition of acto-S1 ATPase. At this R alpha CaP/actin ratio R alpha CaP does not interfere with S1 binding to F-actin. At higher concentrations, R alpha CaP displaces S1 from F-actin and a 1:1 R alpha CaP-actin monomer complex is formed. R alpha CaP is also able to displace troponin I from its complex with F-actin which may reflect the amino acid sequence similarity between R alpha CaP and troponin I in their actin-binding regions.
authors.affiliation: Muscle Research Group, Boston Biomedical Research Institute, MA 02114, USA.
authors.forename: P T
authors.initials: PT
authors.lastname: Szymanski
authors.forename: Z
authors.initials: Z
authors.lastname: Grabarek
authors.forename: T
authors.initials: T
authors.lastname: Tao
mesh_terms: D000199:Actins / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors*; D000818:Animals; D001667:Binding, Competitive; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D002645:Chickens; D008840:Microfilament Proteins; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits; D000096985:Calponins
chemical_list: D000199:Actins; D000251:Adenosine Triphosphatases; D002135:Calcium-Binding Proteins; D008840:Microfilament Proteins; D009218:Myosins; D010446:Peptide Fragments; D000096985:Calponins