Heme-dependent autophosphorylation of a heme sensor kinase, ChrS, from Corynebacterium diphtheriae reconstituted in proteoliposomes

Yoko Ito, Shoko Nakagawa, Ayako Komagata, Masao Ikeda-Saito, Yoshitsugu Shiro, Hiro Nakamura

研究成果: Article査読

25 被引用数 (Scopus)

抄録

Corynebacterium diphteriae employs the response regulator, ChrA, and the sensor kinase, ChrS, of a two-component signal transduction system to utilize host heme iron. Although ChrS is predicted to encode a heme sensor, the sensing mechanism remains to be characterized. In this report, ChrS expressed in Eshcherichia coli membranes was solubilized and purified using decylmaltoside. ChrS protein incorporated into proteoliposomes catalyzed heme-dependent autophosphorylation by ATP. Other metalloporphyrins and iron did not stimulate kinase activity. The UV-Vis spectrum of hemin in the ChrS-proteoliposomes indicated that heme directly interacts with ChrS. This is the first functional reconstitution of a bacterial heme-sensing protein.

本文言語English
ページ(範囲)2244-2248
ページ数5
ジャーナルFEBS Letters
583
13
DOI
出版ステータスPublished - 2009 7月 7

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

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