Purification and characterization of an 'actomyosin' complex from Escherichia coli W3110 |
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Authors: | Simon J. Foster |
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Affiliation: | Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK |
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Abstract: | Abstract An 'actomyosin' complex was purified from Escherichia coli W3110 using selective precipitation. The complex contains three major components of 19.5, 18.5 and 17 kDa. The 19.5- and 17-kDa proteins were purified by electroelution, peptide mapped and N-terminally sequenced. The structural gene for the 17-kDa protein was found to have been previously identified in an operon containing several other genes including the essential lpxA, lpxB and dnaE . The possible function of the 17-kDa protein and the other 'actomyosin' components is discussed. |
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Keywords: | Actomyosin Cytoskeletal elements Escherichia coli |
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