Literature DB >> 11525385

CooA: a heme-containing regulatory protein that serves as a specific sensor of both carbon monoxide and redox state.

G P Roberts1, M V Thorsteinsson, R L Kerby, W N Lanzilotta, T Poulos.   

Abstract

CooA, the heme-containing carbon monoxide (CO) sensor from the bacterium Rhodospirillum rubrum, is a transcriptional factor that activates expression of certain genes in response to CO. As with other heme proteins, CooA is unable to bind CO when the Fe heme is oxidized, consistent with the fact that some of the regulated gene products are oxygen-labile. Upon reduction, there is an unusual switch of protein ligands to the six-coordinate heme and the reduced heme is able to bind CO. CO binding stabilizes a conformation of the dimeric protein that allows sequence-specific DNA binding, and transcription is activated through contacts between CooA and RNA polymerase. CooA is therefore a novel redox sensor as well as a specific CO sensor. CooA is a homolog of catabolite responsive protein (CRP), whose transcriptionally active conformation has been known for some time. The recent solution of the crystal structure of the CO-free (transcriptionally inactive) form of CooA has allowed insights into the mechanism by which both proteins respond to their specific small-molecule effectors.

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Year:  2001        PMID: 11525385     DOI: 10.1016/s0079-6603(01)67024-7

Source DB:  PubMed          Journal:  Prog Nucleic Acid Res Mol Biol        ISSN: 0079-6603


  17 in total

1.  Low frequency spectral density of ferrous heme: perturbations induced by axial ligation and protein insertion.

Authors:  Flaviu Gruia; Xiong Ye; Dan Ionascu; Minoru Kubo; Paul M Champion
Journal:  Biophys J       Date:  2007-08-31       Impact factor: 4.033

2.  Unexpected NO-dependent DNA binding by the CooA homolog from Carboxydothermus hydrogenoformans.

Authors:  Robert W Clark; Nicholas D Lanz; Andrea J Lee; Robert L Kerby; Gary P Roberts; Judith N Burstyn
Journal:  Proc Natl Acad Sci U S A       Date:  2006-01-12       Impact factor: 11.205

3.  Burkholderia xenovorans RcoM(Bx)-1, a transcriptional regulator system for sensing low and persistent levels of carbon monoxide.

Authors:  Robert L Kerby; Gary P Roberts
Journal:  J Bacteriol       Date:  2012-08-24       Impact factor: 3.490

4.  Dual roles of an E-helix residue, Glu167, in the transcriptional activator function of CooA.

Authors:  Hwan Youn; Marc V Thorsteinsson; Mary Conrad; Robert L Kerby; Gary P Roberts
Journal:  J Bacteriol       Date:  2005-04       Impact factor: 3.490

5.  DNA binding by an imidazole-sensing CooA variant is dependent on the heme redox state.

Authors:  Robert W Clark; Hwan Youn; Andrea J Lee; Gary P Roberts; Judith N Burstyn
Journal:  J Biol Inorg Chem       Date:  2006-11-03       Impact factor: 3.358

Review 6.  How do heme-protein sensors exclude oxygen? Lessons learned from cytochrome c', Nostoc puntiforme heme nitric oxide/oxygen-binding domain, and soluble guanylyl cyclase.

Authors:  Ah-Lim Tsai; Emil Martin; Vladimir Berka; John S Olson
Journal:  Antioxid Redox Signal       Date:  2012-04-10       Impact factor: 8.401

7.  Functionally critical elements of CooA-related CO sensors.

Authors:  Hwan Youn; Robert L Kerby; Mary Conrad; Gary P Roberts
Journal:  J Bacteriol       Date:  2004-03       Impact factor: 3.490

Review 8.  CO-sensing mechanisms.

Authors:  Gary P Roberts; Hwan Youn; Robert L Kerby
Journal:  Microbiol Mol Biol Rev       Date:  2004-09       Impact factor: 11.056

9.  Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection.

Authors:  Michael U Shiloh; Paolo Manzanillo; Jeffery S Cox
Journal:  Cell Host Microbe       Date:  2008-05-15       Impact factor: 21.023

Review 10.  Heme sensor proteins.

Authors:  Hazel M Girvan; Andrew W Munro
Journal:  J Biol Chem       Date:  2013-03-28       Impact factor: 5.157

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