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Cited by 28

The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.

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

Ito, Yoko, Nakagawa, Shoko, Komagata, Ayako, Ikeda-Saito, Masao, Shiro, Yoshitsugu, Nakamura, Hiro·2009·FEBS Letters
DOI 10.1016/j.febslet.2009.06.001
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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.

Overview

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Crossref · 10.1016/j.febslet.2009.06.001

Cites

33 of 33 references verified0 citation errors · 0 not checkable

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Citations

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Metadata

Authors
Ito, Y., Nakagawa, S., Komagata, A., Ikeda-Saito, M., Shiro, Y., & Nakamura, H.
Venue
FEBS Letters
Publisher
Wiley
Published
2009-06-08
Volume
583
Issue
13
Pages
2244-2248
ISSN
  • 0014-5793
  • 1873-3468
DOI
10.1016/j.febslet.2009.06.001
Cited by
28
References
33
Language
en
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor)

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Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.