ArticleThe Journal of biological chemistry2015
NsrR from Streptomyces coelicolor is a nitric oxide-sensing [4Fe-4S] cluster protein with a specialized regulatory function.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 91 citations in OpenAlex.
- NRVS of FeS cluster proteins & models - A bestiary of nifty normal modes.Journal of inorganic biochemistry · 2025Review
- ArnR binds a [4Fe-4S] cluster and indirectly senses anaerobicity in Corynebacteria.Metallomics : integrated biometal science · 2025Article
- Nitrite Causes Nitrosative Stress to Iron Sulfur Clusters.Journal of the American Chemical Society · 2025Article
- Identification, Biocontrol and Plant Growth Promotion Potential of Endophytic Streptomyces sp. a13.Current microbiology · 2025Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Fe-S cluster homeostasis and beyond: The multifaceted roles of IscR.Biochimica et biophysica acta. Molecular cell research · 2024Review
- Nitric oxide sensor NsrR is the key direct regulator of magnetosome formation and nitrogen metabolism in Magnetospirillum.Nucleic acids research · 2024Article
- Val43 residue of NsrR is crucial for the nitric oxide response ofMicrobiology spectrum · 2024Article
- Harnessing regulatory networks in Actinobacteria for natural product discovery.Journal of industrial microbiology & biotechnology · 2024Review
- Stabilisation of the RirA [4Fe-4S] cluster results in loss of iron-sensing function.Chemical science · 2023Article
- Comparative Proteomic Analysis of Transcriptional and Regulatory Proteins Abundances inInternational journal of molecular sciences · 2022Article
- The Elusive Mononitrosylated [FeAngewandte Chemie (International ed. in English) · 2022Article
- Structural determinants of DNA recognition by the NO sensor NsrR and related Rrf2-type [FeS]-transcription factors.Communications biology · 2022Article
- The Di-Iron Protein YtfE Is a Nitric Oxide-Generating Nitrite Reductase Involved in the Management of Nitrosative Stress.Journal of the American Chemical Society · 2022Article
- Structural insights into the functional divergence of WhiB-like proteins in Mycobacterium tuberculosis.Molecular cell · 2021Article
- Sensing mechanisms of iron-sulfur cluster regulatory proteins elucidated using native mass spectrometry.Dalton transactions (Cambridge, England : 2003) · 2021Article
- Native Mass Spectrometry of Iron-Sulfur Proteins.Methods in molecular biology (Clifton, N.J.) · 2021Article
- A Nitric Oxide-Responsive Transcriptional Regulator NsrR Cooperates With Lrp and CRP to Tightly Control theFrontiers in microbiology · 2021Article
- System-level understanding of gene expression and regulation for engineering secondary metabolite production in Streptomyces.Journal of industrial microbiology & biotechnology · 2020Review
- SufR, a [4Fe-4S] Cluster-Containing Transcription Factor, Represses theApplied and environmental microbiology · 2020Article
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
Abstract
The Rrf2 family transcription factor NsrR controls expression of genes in a wide range of bacteria in response to nitric oxide (NO). The precise form of the NO-sensing module of NsrR is the subject of controversy because NsrR proteins containing either [2Fe-2S] or [4Fe-4S] clusters have been observed previously. Optical, Mössbauer, resonance Raman spectroscopies and native mass spectrometry demonstrate that Streptomyces coelicolor NsrR (ScNsrR), previously reported to contain a [2Fe-2S] cluster, can be isolated containing a [4Fe-4S] cluster. ChIP-seq experiments indicated that the ScNsrR regulon is small, consisting of only hmpA1, hmpA2, and nsrR itself. The hmpA genes encode NO-detoxifying flavohemoglobins, indicating that ScNsrR has a specialized regulatory function focused on NO detoxification and is not a global regulator like some NsrR orthologues. EMSAs and DNase I footprinting showed that the [4Fe-4S] form of ScNsrR binds specifically and tightly to an 11-bp inverted repeat sequence in the promoter regions of the identified target genes and that DNA binding is abolished following reaction with NO. Resonance Raman data were consistent with cluster coordination by three Cys residues and one oxygen-containing residue, and analysis of ScNsrR variants suggested that highly conserved Glu-85 may be the fourth ligand. Finally, we demonstrate that some low molecular weight thiols, but importantly not physiologically relevant thiols, such as cysteine and an analogue of mycothiol, bind weakly to the [4Fe-4S] cluster, and exposure of this bound form to O2 results in cluster conversion to the [2Fe-2S] form, which does not bind to DNA. These data help to account for the observation of [2Fe-2S] forms of NsrR.
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