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

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)2244-2248
Number of pages5
JournalFEBS Letters
Volume583
Issue number13
DOIs
Publication statusPublished - 2009 Jul 7

Keywords

  • Autophosphorylation
  • Heme sensor
  • Histidine kinase
  • Liposome
  • Two-component system

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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