Involvement of Arg-328, Arg-334 and Arg-342 of DnaA protein in the functional interaction with acidic phospholipids

Yoshihiro Yamaguchi, Masakazu Hase, Masaki Makise, Shinji Mima, Takeshi Yoshimi, Yuichi Ishikawa, Tomofusa Tsuchiya, Tohru Mizushima

研究成果: Article査読

18 被引用数 (Scopus)

抄録

We reported previously that three basic amino acids (Arg-360, Arg-364 and Lys-372) of DnaA protein are essential for its functional interaction with cardiolipin. In this study, we examined the effect of mutation of some basic amino acids in a potential amphipathic helix (from Lys-327 to Ile-345) of DnaA protein on this interaction. ATP binding to the mutant DnaA protein, in which Arg-328, Arg-334 and Arg-342 were changed to acidic amino acids, was less inhibited by cardiolipin than that of the wild-type protein, as was the case for mutant DnaA protein with mutations of Arg-360, Arg-364 and Lys-372. A mutant DnaA protein with mutations of all six basic amino acids showed the most resistance to the inhibition of ATP binding by cardiolipin. These results suggest that Arg-328, Arg-334 and Arg-342, like Arg-360, Arg-364 and Lys-372, are also involved in the functional interaction between DnaA protein and acidic phospholipids.

本文言語English
ページ(範囲)433-438
ページ数6
ジャーナルBiochemical Journal
340
2
DOI
出版ステータスPublished - 1999 6 1

ASJC Scopus subject areas

  • 生化学
  • 分子生物学
  • 細胞生物学

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