Abstract
The interactions of caldesmon and S1 with the C-terminus of actin were examined in co-sedimentation experiments using proteolytically truncated actin. It is shown that removal of 6 residues from the C-terminus of actin reduces the binding of caldesmon by about 50% while improving the binding of S1 to actin. We also show that S1 protects actin's C-terminus from enzymatic cleavage. Both S1 and caldesmon binding to actin are decreased in the presence of an actin C-terminal peptide. These results emphasize the importance of the C-terminus of actin in binding to S1 and caldesmon.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Actins / isolation & purification
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Actins / metabolism*
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Amino Acid Sequence
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Animals
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Calmodulin-Binding Proteins / isolation & purification
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Calmodulin-Binding Proteins / metabolism*
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Enzyme-Linked Immunosorbent Assay
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Fluorescent Dyes
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Immune Sera
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Kinetics
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Molecular Sequence Data
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Muscles / metabolism
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Myosin Subfragments / isolation & purification
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Myosin Subfragments / metabolism*
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Naphthalenesulfonates
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Peptide Fragments / isolation & purification
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Peptide Fragments / metabolism*
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Protein Binding
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Rabbits
Substances
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Actins
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Calmodulin-Binding Proteins
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Fluorescent Dyes
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Immune Sera
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Myosin Subfragments
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Naphthalenesulfonates
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Peptide Fragments
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1,5-I-AEDANS