Myosin and actin from Escherichia coli K12 C600.

J-STAGE
  • NAKAMURA Kayoko
    Department of Chemistry, Faculty of Science, Tokyo Institute of Technology
  • TAKAHASHI Koui
    Department of Animal Science, Faculty of Agriculture, Hokkaido University
  • WATANABE Shizuo
    Department of Chemistry, Faculty of Science, Tokyo Institute of Technology

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Description

Myosin-like protein and actin-like protein from E. coli formed filaments very similar in structure to those of myosin and actin from skeletal muscle. At 0.2M KCl, a large number of "thick filaments" of uniform size (about 0.6-0.7μm long and about 20 nm wide) was present. These thick filaments aggregated as the KCl concentration decreased to less than 0.2M. Filaments of actin-like protein were decorated with muscle heavy meromyosin, showing "arrowheads" The arrowhead structure disappeared in the presence of ATP.<br> A mixture of E. coli myosin-like protein and rabbit skeletal actin exhibited a gelation phenomenon on the addition of ATP. The phenomenon was reversible and showed ATP specificity. However, the gelation phenomenon was not observed with the mixture of E. coli actin-like protein and E. coli myosin-like protein.<br> These results provide compelling evidence that the E. coli myosin-like protein and actin-like protein we isolated are essentially identical to myosin and actin, respectively.

Journal

  • J Biochem (Tokyo)

    J Biochem (Tokyo) 84 (6), 1453-1458, 1978

    The Japanese Biochemical Society

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