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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

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.[1]

References

  1. Identification of a 180 kD protein in Escherichia coli related to a yeast heavy-chain myosin. Casaregola, S., Norris, V., Goldberg, M., Holland, I.B. Mol. Microbiol. (1990) [Pubmed]
 
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