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  • Title: An intact heavy chain at the actin-subfragment 1 interface is required for ATPase activity of scallop myosin.
    Author: Szentkiralyi EM.
    Journal: J Muscle Res Cell Motil; 1987 Aug; 8(4):349-57. PubMed ID: 2958500.
    Abstract:
    Scallop S1 has a region sensitive to tryptic hydrolysis not found thus far in S1s of other species, located 65K from the N-terminus as determined by SDS/polyacrylamide-gel electrophoresis. In the presence of actin the S1 heavy chain is preferentially cleaved at this site. The high-salt EDTA and calcium ATPase activities of the nicked 65K-31K S1 are abolished. This inactivation is not due to denaturation, conformational effects of actin, or to light chain dissociation. The unique proteolytic site of scallop S1 is adjacent to a peptide involved in actin-S1 interaction in scallop and rabbit but it is far removed from the nucleotide-binding site in the linear amino acid sequence. We conclude that proteolysis inactivates the high-salt ATPase activities through a connection mediated by tertiary interactions. Such a connection provides a structural correlate for the known reciprocal relationship between the nucleotide and actin affinities of myosin.
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