ArticleCommunications biology2022
Structural determinants of DNA recognition by the NO sensor NsrR and related Rrf2-type [FeS]-transcription factors.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Nitrite Causes Nitrosative Stress to Iron Sulfur Clusters.Journal of the American Chemical Society · 2025Article
- Iron-sulfur protein odyssey: exploring their cluster functional versatility and challenging identification.Metallomics : integrated biometal science · 2024Review
- Evolution of triclosan resistance modulates bacterial permissiveness to multidrug resistance plasmids and phages.Nature communications · 2024Article
- Val43 residue of NsrR is crucial for the nitric oxide response ofMicrobiology spectrum · 2024Article
- Genome-scale identification and comparative analysis of transcription factors in thermophilic cyanobacteria.BMC genomics · 2024Article
- Metalloprotein enabled redox signal transduction in microbes.Current opinion in chemical biology · 2023Review
- Stabilisation of the RirA [4Fe-4S] cluster results in loss of iron-sensing function.Chemical science · 2023Article
- Article
- The Elusive Mononitrosylated [FeAngewandte Chemie (International ed. in English) · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Several transcription factors of the Rrf2 family use an iron-sulfur cluster to regulate DNA binding through effectors such as nitric oxide (NO), cellular redox status and iron levels. [4Fe-4S]-NsrR from Streptomyces coelicolor (ScNsrR) modulates expression of three different genes via reaction and complex formation with variable amounts of NO, which results in detoxification of this gas. Here, we report the crystal structure of ScNsrR complexed with an hmpA1 gene operator fragment and compare it with those previously reported for [2Fe-2S]-RsrR/rsrR and apo-IscR/hyA complexes. Important structural differences reside in the variation of the DNA minor and major groove widths. In addition, different DNA curvatures and different interactions with the protein sensors are observed. We also report studies of NsrR binding to four hmpA1 variants, which indicate that flexibility in the central region is not a key binding determinant. Our study explores the promotor binding specificities of three closely related transcriptional regulators.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.