TY - JOUR
T1 - Involvement of Arg-328, Arg-334 and Arg-342 of DnaA protein in the functional interaction with acidic phospholipids
AU - Yamaguchi, Yoshihiro
AU - Hase, Masakazu
AU - Makise, Masaki
AU - Mima, Shinji
AU - Yoshimi, Takeshi
AU - Ishikawa, Yuichi
AU - Tsuchiya, Tomofusa
AU - Mizushima, Tohru
PY - 1999/6/1
Y1 - 1999/6/1
N2 - 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.
AB - 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.
KW - Basic amino acid
KW - Escherichia coli
KW - Initiator protein
KW - Membrane binding
KW - Site-directed mutagenesis
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U2 - 10.1042/0264-6021:3400433
DO - 10.1042/0264-6021:3400433
M3 - Article
C2 - 10333486
AN - SCOPUS:0033153493
SN - 0264-6021
VL - 340
SP - 433
EP - 438
JO - Biochemical Journal
JF - Biochemical Journal
IS - 2
ER -