We have determined the primary structure of a myosin I (called mammalian myosin Iβ, MMIβ) from bovine brain and identified its functional domains. The protein was previously purified from brain and adrenal gland. Several constructs were generated and expressed in Escherichia coli as glutathione S- transferase fusion proteins and the recombinant proteins were recognized by monoclonal antibodies that recognize either 'head' or 'tail' domains of native myosin I. A gel overlay method was used to confirm that calmodulin binds to the consensus calmodulin-binding sequence in MMIβ. Binding assays were used to detect interaction with anionic phospholipid vesicles. We conclude that MMIβ consists of an amino-terminal 80.5-kDa domain that contains the ATP- and actin-binding sites, followed by an 8.5-kDa domain with three calmodulin-binding sequences and a basic 30-kDa carboxyl-terminal tail segment that binds to anionic phospholipids and membranes.
|Original language||English (US)|
|Number of pages||5|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|State||Published - Jul 5 1994|
- calmodulin binding
- phospholipid binding
ASJC Scopus subject areas