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Heme‐dependent autophosphorylation of a heme sensor kinase, ChrS, from Corynebacterium diphtheriae reconstituted in proteoliposomes
Author(s) -
Ito Yoko,
Nakagawa Shoko,
Komagata Ayako,
Ikeda-Saito Masao,
Shiro Yoshitsugu,
Nakamura Hiro
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.06.001
Subject(s) - heme , hemin , autophosphorylation , histidine kinase , biochemistry , chemistry , biology , protein kinase a , microbiology and biotechnology , kinase , enzyme , histidine
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.