Abstract
A 17 kDa protein, designated as coactosin, has been purified from an actin-myosin complex reconstituted in vitro from a soluble fraction of Dictyostelium discoideum cells. The protein binds to F-actin in vitro without significantly altering its viscosity. Immunoblots labeled with monoclonal antibodies indicate that part of the protein is associated with the detergent-insoluble cytoskeleton. cDNA clones comprising the entire coding region of coactosin have been isolated from an expression library. The cDNA-derived amino-acid sequence reveals similarities of coactosin to the drebrins identified in neurons and to actin-binding proteins from other organisms, including yeast ABP1p, and yeast and vertebrate cofilins.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actomyosin / metabolism
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Amino Acid Sequence
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Animals
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Antibodies, Monoclonal / immunology
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Artifacts
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Base Sequence
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Cytoplasm / chemistry
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DNA, Complementary / immunology
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Dictyostelium / chemistry*
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Dictyostelium / genetics
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Fixatives / pharmacology
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Fungal Proteins / genetics
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Fungal Proteins / immunology
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Fungal Proteins / isolation & purification*
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Fungal Proteins / metabolism
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Microfilament Proteins / genetics
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Microfilament Proteins / immunology
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Microfilament Proteins / isolation & purification*
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Microfilament Proteins / metabolism
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Molecular Sequence Data
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Protozoan Proteins*
Substances
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Antibodies, Monoclonal
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DNA, Complementary
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Fixatives
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Fungal Proteins
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Microfilament Proteins
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Protozoan Proteins
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coactosin protein, Dictyostelium discoideum
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Actomyosin