Identification of a 180 kD protein in Escherichia coli related to a yeast heavy-chain myosin.
A high molecular-weight protein from Escherichia coli sharing structural homology at the protein level with a yeast heavy-chain myosin encoded by the MYO1 gene is described. This 180 kD protein (180-HMP) can be enriched in cell fractions following the procedure normally utilized for the purification of non-muscle myosins. In Western blots this protein cross-reacts with a monoclonal antibody against yeast heavy-chain myosin. Moreover, antibodies raised against the 180 kD protein cross-react with the yeast myosin and with a myosin heavy chain from chicken. Recognition by anti-180-HMP antibodies of an overexpressed fragment of yeast myosin encoded by MYO1 allows the localization of one of the shared epitopes to a specific region around the ATP binding site of the yeast myosin heavy chain. The existence of a high molecular-weight protein with structural similarity to myosin in E. coli raises the possibility that such a protein might generate the force required for movement in processes such as nucleoid segregation and cell division.
Department of Genetics, University of Leicester, UK.
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Casaregola
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Norris
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Goldberg
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Holland
D000942:Antigens, Bacterial / Q000276:immunology; D001426:Bacterial Proteins / Q000302:isolation & purification*; D005075:Biological Evolution; D003429:Cross Reactions; D004926:Escherichia coli / Q000032:analysis* / Q000276:immunology; D008970:Molecular Weight; D009218:Myosins / Q000032:analysis* / Q000276:immunology; D012441:Saccharomyces cerevisiae / Q000032:analysis*
D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D009218:Myosins