Design and functional analysis of actomyosin motor domain chimera proteins

Keiichi Yokoyama, Yuichi Hiratuka, Erika Akimaru, Keiko Hirose, Taro Q.P. Uyeda, Makoto Suzuki*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


To gain more structural and functional information on the actomyosin complexes, we have engineered chimera proteins carrying the entire Dictyostelium actin in the loop 2 sequence of the motor domain of Dictyostelium myosin II. Although the chimera proteins were unable to polymerize by themselves, addition of skeletal actin promoted polymerization. Electron microscopic observation demonstrated that the chimera proteins were incorporated into actin filaments, when copolymerized with skeletal actin. Copolymerization with skeletal actin greatly enhanced the MgATPase, while the chimera proteins without added skeletal actin hydrolyzed ATP at a very low rate. These results indicate that the actin part and the motor domain part of the chimera proteins are correctly folded, but the chimera proteins are structurally stressed so that efficient polymerization is inhibited.

Original languageEnglish
Pages (from-to)825-831
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number5
Publication statusPublished - 2002
Externally publishedYes


  • ATPase
  • Dictyostelium
  • Electron microscopy
  • Loop 2
  • Pelleting assay

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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