In vivo analysis of dimer formation of a circadian input factor Pex

DOI
  • Kutsuna Shinsuke
    Graduate School of International Arts and Sciences, Yokohama City Univ.
  • Manabe Katsushi
    Graduate School of International Arts and Sciences, Yokohama City Univ.
  • Arita Kyouhei
    Graduate School of International Arts and Sciences, Yokohama City Univ.
  • Sato Mamoru
    Graduate School of International Arts and Sciences, Yokohama City Univ.
  • Shimizu Toshiyuki
    Graduate School of International Arts and Sciences, Yokohama City Univ.

Bibliographic Information

Other Title
  • ラン藻の概日リズム入力系因子Pexの2量体解析

Abstract

A circadian clock resetting protein Pex in the cyanobacterium Synechococcus elongatus PCC 7942 accumulates dark condition and regulates the phase and period of the rhythm. Pex binds to the promoter of the clock essential gene kaiA, whose protein KaiA accelerates the phosphorylation of KaiC protein and shortens the circadian cycle. Then, Pex represses the expression of the clock gene. An alpha helix and a positively charged loop between two beta sheets in Pex is essential to bind the promoter in vitro and the in vivo period regulation. Here, we examined molecular weight of Pex in vivo by gel-filtration method and determined as 25 kD in size, suggesting Pex dimer because its monomer shows 13.1 kDa in SDS polyacrylamide gel. Then, we also show the importance of the dimer formation by using bioluminescence rhythm monitoring method and several reporter strains expressing an amino acid replaced Pex protein.

Journal

Details 詳細情報について

  • CRID
    1390001205629971968
  • NII Article ID
    130006990455
  • DOI
    10.14841/jspp.2008.0.0499.0
  • Data Source
    • JaLC
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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