ArticleNucleic acids research2024
Structural basis for transcription activation by the nitrate-responsive regulator NarL.
Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- Binding analysis of the response regulator NarL protein to the promoter of the OMolecular biology reports · 2026Article
- Molecular basis of DosR-dependent transcription activation in Mycobacterium tuberculosis.Nature communications · 2026Article
- Thermal modulation of transcriptional states, biofilm architecture and survival strategies inFrontiers in microbiology · 2026Article
- In Hyphomicrobium denitrificans Two Related Sulfane-Sulfur Responsive Transcriptional Repressors Regulate Thiosulfate Oxidation and Have a Deep Impact on Nitrate Respiration and Anaerobic Biosyntheses.Molecular microbiology · 2025Article
- UropathogenicInternational journal of molecular sciences · 2025Article
- Plant Growth-Promoting Effect and Complete Genomic Sequence Analysis of the Beneficial RhizosphereMicroorganisms · 2025Article
- ChIP-seq and structural analyses delineating the regulatory mechanism of master regulator EsrB inApplied and environmental microbiology · 2024Article
- Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Transcription activation is a crucial step of regulation during transcription initiation and a classic check point in response to different stimuli and stress factors. The Escherichia coli NarL is a nitrate-responsive global transcription factor that controls the expression of nearly 100 genes. However, the molecular mechanism of NarL-mediated transcription activation is not well defined. Here we present a cryo-EM structure of NarL-dependent transcription activation complex (TAC) assembled on the yeaR promoter at 3.2 Å resolution. Our structure shows that the NarL dimer binds at the -43.5 site of the promoter DNA with its C-terminal domain (CTD) not only binding to the DNA but also making interactions with RNA polymerase subunit alpha CTD (αCTD). The key role of these NarL-mediated interactions in transcription activation was further confirmed by in vivo and in vitro transcription assays. Additionally, the NarL dimer binds DNA in a different plane from that observed in the structure of class II TACs. Unlike the canonical class II activation mechanism, NarL does not interact with σ4, while RNAP αCTD is bound to DNA on the opposite side of NarL. Our findings provide a structural basis for detailed mechanistic understanding of NarL-dependent transcription activation on yeaR promoter and reveal a potentially novel mechanism of transcription activation.
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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 Socratic graph.