Abstract
The interface between gizzard filamin and skeletal muscle actin was located on the actin monomer. Conserved sequences 105-120 and 360-372, in the actin subdomain 1 near the myosin binding sites, were involved in this interaction. The corresponding peptides for these sequences were each found to bind filamin and compete in the actin-filamin interaction. When these two peptides were used together in the presence of filamin and filamentous actin, they dissociated sedimentable complexes formed by these two proteins.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actins / chemistry*
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Actins / metabolism*
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Amino Acid Sequence
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Animals
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Carrier Proteins / metabolism
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Chickens
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Contractile Proteins / isolation & purification
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Contractile Proteins / metabolism*
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Electrophoresis, Polyacrylamide Gel
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Filamins
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Fluorescent Dyes
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Kinetics
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Microfilament Proteins / isolation & purification
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Microfilament Proteins / metabolism*
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Muscle, Smooth / metabolism
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Muscles / metabolism
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Naphthalenesulfonates
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Peptide Fragments / isolation & purification
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Protein Binding
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Rabbits
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Tropomyosin / metabolism
Substances
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Actins
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Carrier Proteins
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Contractile Proteins
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Filamins
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Fluorescent Dyes
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Microfilament Proteins
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Naphthalenesulfonates
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Peptide Fragments
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Tropomyosin
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1,5-I-AEDANS