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
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.
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“Another heme-responsive TCS distinct from HssRS is ChrAS from Corynebacterium diphtheriae (46).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [46]
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Self-citation
Cited by
Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens
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Control of Heme Homeostasis in Corynebacterium glutamicum by the Two-Component System HrrSA
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Bibb, L. A., & Schmitt, M. P. (2010) · Journal of Bacteriology · doi:10.1128/jb.00525-10 · Cited by 59
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
- Cited by
- 28
- References
- 33
- Language
- en
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