The transcriptional repressor protein NsrR senses nitric oxide directly via a [2Fe-2S] cluster
The regulatory protein NsrR, a member of the Rrf2 family of transcription repressors, is specifically dedicated to sensing nitric oxide (NO) in a variety of pathogenic and non-pathogenic bacteria. It has been proposed that NO directly modulates NsrR activity by interacting with a predicted [Fe-S] cl...
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Published in | PloS one Vol. 3; no. 11; p. e3623 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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Public Library of Science
07.11.2008
Public Library of Science (PLoS) |
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Abstract | The regulatory protein NsrR, a member of the Rrf2 family of transcription repressors, is specifically dedicated to sensing nitric oxide (NO) in a variety of pathogenic and non-pathogenic bacteria. It has been proposed that NO directly modulates NsrR activity by interacting with a predicted [Fe-S] cluster in the NsrR protein, but no experimental evidence has been published to support this hypothesis. Here we report the purification of NsrR from the obligate aerobe Streptomyces coelicolor. We demonstrate using UV-visible, near UV CD and EPR spectroscopy that the protein contains an NO-sensitive [2Fe-2S] cluster when purified from E. coli. Upon exposure of NsrR to NO, the cluster is nitrosylated, which results in the loss of DNA binding activity as detected by bandshift assays. Removal of the [2Fe-2S] cluster to generate apo-NsrR also resulted in loss of DNA binding activity. This is the first demonstration that NsrR contains an NO-sensitive [2Fe-2S] cluster that is required for DNA binding activity. |
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AbstractList | The regulatory protein NsrR, a member of the Rrf2 family of transcription repressors, is specifically dedicated to sensing nitric oxide (NO) in a variety of pathogenic and non-pathogenic bacteria. It has been proposed that NO directly modulates NsrR activity by interacting with a predicted [Fe-S] cluster in the NsrR protein, but no experimental evidence has been published to support this hypothesis. Here we report the purification of NsrR from the obligate aerobe Streptomyces coelicolor. We demonstrate using UV-visible, near UV CD and EPR spectroscopy that the protein contains an NO-sensitive [2Fe-2S] cluster when purified from E. coli. Upon exposure of NsrR to NO, the cluster is nitrosylated, which results in the loss of DNA binding activity as detected by bandshift assays. Removal of the [2Fe-2S] cluster to generate apo-NsrR also resulted in loss of DNA binding activity. This is the first demonstration that NsrR contains an NO-sensitive [2Fe-2S] cluster that is required for DNA binding activity. The regulatory protein NsrR, a member of the Rrf2 family of transcription repressors, is specifically dedicated to sensing nitric oxide (NO) in a variety of pathogenic and non-pathogenic bacteria. It has been proposed that NO directly modulates NsrR activity by interacting with a predicted [Fe-S] cluster in the NsrR protein, but no experimental evidence has been published to support this hypothesis. Here we report the purification of NsrR from the obligate aerobe Streptomyces coelicolor . We demonstrate using UV-visible, near UV CD and EPR spectroscopy that the protein contains an NO-sensitive [2Fe-2S] cluster when purified from E. coli . Upon exposure of NsrR to NO, the cluster is nitrosylated, which results in the loss of DNA binding activity as detected by bandshift assays. Removal of the [2Fe-2S] cluster to generate apo-NsrR also resulted in loss of DNA binding activity. This is the first demonstration that NsrR contains an NO-sensitive [2Fe-2S] cluster that is required for DNA binding activity. |
Audience | Academic |
Author | Le Brun, Nick E Dixon, Ray Hicks, Matthew G Tucker, Nicholas P Chandra, Govind Clarke, Thomas A Crack, Jason C Hutchings, Matthew I |
AuthorAffiliation | 3 School of Chemical Sciences and Pharmacy, University of East Anglia, Norwich Research Park, Norwich, United Kingdom 1 Department of Molecular Microbiology, John Innes Centre, Norwich Research Park, Norwich, United Kingdom 2 School of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich, United Kingdom Temasek Life Sciences Laboratory, Singapore 4 School of Medicine, Health Policy and Practice, University of East Anglia, Norwich Research Park, Norwich, United Kingdom |
AuthorAffiliation_xml | – name: 3 School of Chemical Sciences and Pharmacy, University of East Anglia, Norwich Research Park, Norwich, United Kingdom – name: Temasek Life Sciences Laboratory, Singapore – name: 1 Department of Molecular Microbiology, John Innes Centre, Norwich Research Park, Norwich, United Kingdom – name: 4 School of Medicine, Health Policy and Practice, University of East Anglia, Norwich Research Park, Norwich, United Kingdom – name: 2 School of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich, United Kingdom |
Author_xml | – sequence: 1 givenname: Nicholas P surname: Tucker fullname: Tucker, Nicholas P email: nick.tucker@bbsrc.ac.uk organization: Department of Molecular Microbiology, John Innes Centre, Norwich Research Park, Norwich, United Kingdom. nick.tucker@bbsrc.ac.uk – sequence: 2 givenname: Matthew G surname: Hicks fullname: Hicks, Matthew G – sequence: 3 givenname: Thomas A surname: Clarke fullname: Clarke, Thomas A – sequence: 4 givenname: Jason C surname: Crack fullname: Crack, Jason C – sequence: 5 givenname: Govind surname: Chandra fullname: Chandra, Govind – sequence: 6 givenname: Nick E surname: Le Brun fullname: Le Brun, Nick E – sequence: 7 givenname: Ray surname: Dixon fullname: Dixon, Ray – sequence: 8 givenname: Matthew I surname: Hutchings fullname: Hutchings, Matthew I |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/18989365$$D View this record in MEDLINE/PubMed |
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ContentType | Journal Article |
Copyright | COPYRIGHT 2008 Public Library of Science 2008 Tucker et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. Tucker et al. 2008 |
Copyright_xml | – notice: COPYRIGHT 2008 Public Library of Science – notice: 2008 Tucker et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. – notice: Tucker et al. 2008 |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Conceived and designed the experiments: NPT MGH TAC NELB RD MIH. Performed the experiments: NPT MGH TAC JCC MIH. Analyzed the data: NPT TAC JCC NELB RD MIH. Contributed reagents/materials/analysis tools: TAC NELB RD MIH. Wrote the paper: NPT TAC JCC NELB RD MIH. Performed the bioinformatic analysis: GC. |
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SubjectTerms | Amino Acid Sequence Bacillus subtilis Bacteria Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Binding Binding Sites Biochemistry/Protein Chemistry Blood proteins Clusters Deoxyribonucleic acid DNA DNA - metabolism DNA binding E coli Electron Spin Resonance Spectroscopy Genes Genetic aspects Genetic research Iron-Sulfur Proteins - chemistry Iron-Sulfur Proteins - isolation & purification Iron-Sulfur Proteins - metabolism Ligands Microbiology Molecular Biology/Transcription Initiation and Activation Molecular Sequence Data Mycobacterium tuberculosis Nitrates Nitric oxide Nitric Oxide - metabolism Pharmacy Proteins Pseudomonas Repressor Proteins - chemistry Repressor Proteins - isolation & purification Repressor Proteins - metabolism Repressors Research parks Salmonella Salmonella Typhimurium Sequence Alignment Spectroscopy Spectroscopy, Mossbauer Streptomyces Streptomyces coelicolor - metabolism Transcription (Genetics) Transcription factors Transcription, Genetic Tuberculosis |
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Title | The transcriptional repressor protein NsrR senses nitric oxide directly via a [2Fe-2S] cluster |
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