Abstract
Site-specific proteases and antisera to the amino terminus of villin have been used to show that villin is organized into seven protease-resistant domains. Six are contained in the amino-terminal Mr 87,000 villin core, a Ca2+-regulated actin-severing fragment, whereas the carboxyl-terminal domain includes the villin "headpiece," a fragment involved in bundling of actin filaments. Ca2+ inhibits proteolytic cleavage between domains in the amino-terminal half of villin. The protein sequence of villin deduced from a single cDNA clone contains a conserved sequence that is repeated six times and is found in each domain of the villin core. The conserved repeats are found in other actin-severing proteins but not in the villin headpiece. Our results suggest that actin-severing proteins are organized around a common Mr 14,000-17,000 domain.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Calcium / pharmacology
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Calcium-Binding Proteins
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Carrier Proteins* / genetics
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Carrier Proteins* / metabolism
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Chickens
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Chymotrypsin / metabolism
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DNA / genetics
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Electrophoresis, Polyacrylamide Gel
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Gelsolin
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Immunoassay
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Microfilament Proteins* / genetics
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Microfilament Proteins* / metabolism
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Molecular Sequence Data
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Molecular Weight
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Peptide Fragments / metabolism
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Repetitive Sequences, Nucleic Acid
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Sequence Homology, Nucleic Acid
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Serine Endopeptidases / metabolism
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Trypsin / metabolism
Substances
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Calcium-Binding Proteins
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Carrier Proteins
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Gelsolin
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Microfilament Proteins
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Peptide Fragments
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villin
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DNA
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Serine Endopeptidases
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Chymotrypsin
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glutamyl endopeptidase
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Trypsin
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Calcium
Associated data
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GENBANK/J03781
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PIR/UNKNOWN