ArticleChemistry & biology2008
A full-length group 1 bacterial sigma factor adopts a compact structure incompatible with DNA binding.
Article in Chemistry & biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 63 citations in OpenAlex.
- Substitutions in RNA-binding protein Hrp1 map a potential interaction surface with the yeast RNA polymerase II elongation complex.Genetics · 2026Article
- Differential association of primary and alternative σ factors with RNA polymerase of Mycobacterium tuberculosis during transcription elongation.Nucleic acids research · 2026Article
- Article
- MoaB2, a newly identified transcription factor, binds to σJournal of bacteriology · 2024Article
- Mycobacterial HelD connects RNA polymerase recycling with transcription initiation.Nature communications · 2024Article
- Evidence for a compact σiScience · 2024Article
- Structural Insight into the Mechanism of σ32-Mediated Transcription Initiation of Bacterial RNA Polymerase.Biomolecules · 2023Article
- The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling.Nature communications · 2020Article
- Rewiring of growth-dependent transcription regulation by a point mutation in region 1.1 of the housekeeping σ factor.Nucleic acids research · 2020Article
- The C-terminal tails of the mitochondrial transcription factors Mtf1 and TFB2M are part of an autoinhibitory mechanism that regulates DNA binding.The Journal of biological chemistry · 2020Article
- The σ Subunit-Remodeling Factors: An Emerging Paradigms of Transcription Regulation.Frontiers in microbiology · 2020Review
- Structural basis for transcription activation by Crl through tethering of σProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Diversity, versatility and complexity of bacterial gene regulation mechanisms: opportunities and drawbacks for applications in synthetic biology.FEMS microbiology reviews · 2019Review
- The Core and Holoenzyme Forms of RNA Polymerase fromJournal of bacteriology · 2019Article
- Single-molecule analysis reveals the mechanism of transcription activation inScience advances · 2018Article
- Solution structure of domain 1.1 of the σThe Journal of biological chemistry · 2017Article
- Structural insights into the mycobacteria transcription initiation complex from analysis of X-ray crystal structures.Nature communications · 2017Article
- Crystal structure ofProceedings of the National Academy of Sciences of the United States of America · 2017Article
- E. coli RNA Polymerase Determinants of Open Complex Lifetime and Structure.Journal of molecular biology · 2015Article
- Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function and Distribution.Biomolecules · 2015Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The sigma factors are the key regulators of bacterial transcription initiation. Through direct read-out of promoter DNA sequence, they recruit the core RNA polymerase to sites of initiation, thereby dictating the RNA polymerase promoter-specificity. The group 1 sigma factors, which direct the vast majority of transcription initiation during log phase growth and are essential for viability, are autoregulated by an N-terminal sequence known as sigma1.1. We report the solution structure of Thermotoga maritima sigmaA sigma1.1. We additionally demonstrate by using chemical crosslinking strategies that sigma1.1 is in close proximity to the promoter recognition domains of sigmaA. We therefore propose that sigma1.1 autoinhibits promoter DNA binding of free sigmaA by stabilizing a compact organization of the sigma factor domains that is unable to bind DNA.
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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.