Purification and characterization of an 'actomyosin' complex from Escherichia coli W3110.
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.
Foster
S J
SJ
Department of Molecular Biology and Biotechnology, University of Sheffield, UK.
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
D000205:Actomyosin; D006836:Hydro-Lyases; C047118:3-hydroxyacyl-(acyl-carrier-protein) dehydratase; D054889:Fatty Acid Synthase, Type II