A synthetic peptide of the N-terminus of actin interacts with myosin.
Research reported from numerous laboratories suggested that the N-terminal region of actin contained one of the binding sites between actin and myosin. A synthetic peptide corresponding to residues 1-28 of skeletal actin was prepared by solid-phase peptide methodology. The formation of a complex between this peptide and myosin subfragment 1 (S1) was demonstrated by high-performance size-exclusion chromatography (pH 6.8). The actin peptide precipitated S1 at higher pH (7.4-8.2) but remained soluble when bound to heavy meromyosin (HMM) or S1 in the presence of F-actin. The actin peptide 1-28 bound to S1 and HMM and activated the ATPase activity in a manner similar to that of F-actin. These results demonstrate that the N-terminal region of actin, residues 1-28, contains a biologically important binding site for myosin.
Van Eyk
J E
JE
Department of Biochemistry, University of Alberta, Edmonton, Canada.
Hodges
R S
RS
D000199:Actins / Q000138:chemical synthesis / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D009132:Muscles / Q000378:metabolism; D009218:Myosins / Q000378:metabolism*; D011817:Rabbits
D000199:Actins; D000251:Adenosine Triphosphatases; D009218:Myosins