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

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)433-438
Number of pages6
JournalBiochemical Journal
Volume340
Issue number2
DOIs
Publication statusPublished - 1999 Jun 1

Keywords

  • Basic amino acid
  • Escherichia coli
  • Initiator protein
  • Membrane binding
  • Site-directed mutagenesis

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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