Involvement of an arginine residue of actin in tropomyosin binding. |
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Authors: | P Johnson J M Blazyk |
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Institution: | Department of Chemistry Ohio University Athens, Ohio 45701, U.S.A. |
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Abstract: | Using 1,2-cyclohexanedione, modification of three arginines per actin monomer in F-actin resulted in a loss of ability of the actin to interact with tropomyosin, although the F-actin polymer was not significantly depolymerized, the ability of the actin to activate the Mg2+-ATPase of myosin was not affected, and the secondary structure of the actin monomers was not appreciably altered. Isolation of peptides from a digest of modified F-actin indicated that the modified residues were Arg-28, Arg-95 and Arg-147. When actin was combined with tropomyosin prior to the modification treatment, Arg-95 was not modified, and the actin retained its ability to bind tropomyosin. These results therefore indicate a direct involvement of Arg-95 in the tropomyosin binding function of F-actin. |
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