Sequence similarities between chicken intestinal 110-kDa ATPase and myosin I-like enzymes |
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Authors: | Mark A. L. Atkinson and Jimmy H. Collins |
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Affiliation: | (1) Department of Biochemistry, University of Texas Health Center at Tyler, P. O. Box 2003, 75710 Tyler, Texas;(2) Department of Microbiology, Biochemistry and Molecular Biology, University of Pittsburgh School of Medicine, 15261 Pittsburgh, Pennsylvania |
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Abstract: | We report the partial amino acid sequence of chicken intestinal microvillar 110-kDa protein that, as a complex with calmodulin, has previously been shown to exhibit myosin-like ATPase and actin-binding activities. The sequence shows a high degree of similarity to the sequence of a novel vertebrate myosin I-like heavy chain encoded by a cDNA isolated from bovine intestine. This confirms that the bovine and chicken proteins are the first examples of Acanthamoeba myosin I-like proteins from higher eukaryotes. Comparison of available structural and functional data leads us to postulate that the myosin I family of proteins result from the fusion of a conserved myosin headlike motor domain, with variable COOH-terminal domains responsible for binding to specific intracellular structures. |
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Keywords: | myosin amino acid sequence homology intestinal microvilli |
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