title: Purification and characterization of an 'actomyosin' complex from Escherichia coli W3110.
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.
authors.affiliation: Department of Molecular Biology and Biotechnology, University of Sheffield, UK.
authors.forename: S J
authors.initials: SJ
authors.lastname: Foster
mesh_terms: D000205:Actomyosin / Q000235:genetics* / Q000302:isolation & purification; D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000235:genetics*; D054889:Fatty Acid Synthase, Type II; D005798:Genes, Bacterial / Q000235:genetics*; D006836:Hydro-Lyases / Q000235:genetics; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
chemical_list: D000205:Actomyosin; D006836:Hydro-Lyases; C047118:3-hydroxyacyl-(acyl-carrier-protein) dehydratase; D054889:Fatty Acid Synthase, Type II