NDLI: Differentiated, Promoter-specific Response of [4Fe-4S] NsrR DNA Binding to Reaction with Nitric $Oxide^{*}$

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Differentiated, Promoter-specific Response of [4Fe-4S] NsrR DNA Binding to Reaction with Nitric $Oxide^{*}$

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Crack, Jason C. Svistunenko, Dimitri A. Munnoch, John Thomson, Andrew J. Hutchings, Matthew I. Le Brun, Nick E.
Description	Author Affiliation: Crack JC ( From the Centre for Molecular and Structural Biochemistry, School of Chemistry, and.); Svistunenko DA ( the School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, United Kingdom.); Munnoch J ( the School of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ and.); Thomson AJ ( From the Centre for Molecular and Structural Biochemistry, School of Chemistry, and.); Hutchings MI ( the School of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ and.); Le Brun NE ( From the Centre for Molecular and Structural Biochemistry, School of Chemistry, and n.le-brun@uea.ac.uk.)
Abstract	NsrR is an iron-sulfur cluster protein that regulates the nitric oxide (NO) stress response of many bacteria. NsrR from Streptomyces coelicolor regulates its own expression and that of only two other genes, hmpA1 and hmpA2, which encode HmpA enzymes predicted to detoxify NO. NsrR binds promoter DNA with high affinity only when coordinating a [4Fe-4S] cluster. Here we show that reaction of [4Fe-4S] NsrR with NO affects DNA binding differently depending on the gene promoter. Binding to the hmpA2 promoter was abolished at ∼2 NO per cluster, although for the hmpA1 and nsrR promoters, ∼4 and ∼8 NO molecules, respectively, were required to abolish DNA binding. Spectroscopic and kinetic studies of the NO reaction revealed a rapid, multi-phase, non-concerted process involving up to 8–10 NO molecules per cluster, leading to the formation of several iron-nitrosyl species. A distinct intermediate was observed at ∼2 NO per cluster, along with two further intermediates at ∼4 and ∼6 NO. The NsrR nitrosylation reaction was not significantly affected by DNA binding. These results show that NsrR regulates different promoters in response to different concentrations of NO. Spectroscopic evidence indicates that this is achieved by different NO-FeS complexes.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	16
Volume Number	291
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2016-04-15
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Metabolism DNA, Bacterial Iron-Sulfur Proteins Nitric Oxide Promoter Regions, Genetic Physiology Streptomyces Coelicolor Transcription Factors Genetics Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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