The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP-DnaA-specific initiation complexes

Kenji Keyamura, Norie Fujikawa, Takuma Ishida, Shogo Ozaki, Masayuki Su'etsugu, Kazuyuki Fujimitsu, Wataru Kagawa, Shigeyuki Yokoyama, Hitoshi Kurumizaka, Tsutomu Katayama*

*この研究の対応する著者

    研究成果: Article査読

    97 被引用数 (Scopus)

    抄録

    Escherichia coli DiaA is a DnaA-binding protein that is required for the timely initiation of chromosomal replication during the cell cycle. In this study, we determined the crystal structure of DiaA at 1.8 Å resolution. DiaA forms a homotetramer consisting of a symmetrical pair of homodimers. Mutational analysis revealed that the DnaA-binding activity and formation of homotetramers are required for the stimulation of initiation by DiaA. DiaA tetramers can bind multiple DnaA molecules simultaneously. DiaA stimulated the assembly of multiple DnaA molecules on oriC, conformational changes in ATP-DnaA-specific initiation complexes, and unwinding of oriC duplex DNA. The mutant DiaA proteins are defective in these stimulations. DiaA associated also with ADP-DnaA, and stimulated the assembly of inactive ADP-DnaA-oriC complexes. Specific residues in the putative phosphosugar-binding motif of DiaA were required for the stimulation of initiation and formation of ATP-DnaA-specific- oriC complexes. Our data indicate that DiaA regulates initiation by a novel mechanism, in which DiaA tetramers most likely bind to multiple DnaA molecules and stimulate the assembly of specific ATP-DnaA-oriC complexes. These results suggest an essential role for DiaA in the promotion of replication initiation in a cell cycle coordinated manner.

    本文言語English
    ページ(範囲)2083-2099
    ページ数17
    ジャーナルGenes and Development
    21
    16
    DOI
    出版ステータスPublished - 2007 8月 15

    ASJC Scopus subject areas

    • 遺伝学
    • 発生生物学

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