ArticleJournal of molecular biology2007
Crystal structure of the Escherichia coli regulator of sigma70, Rsd, in complex with sigma70 domain 4.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
38 citing papers in PubMed, 60 citations in OpenAlex.
- Article
- MoaB2, a newly identified transcription factor, binds to σJournal of bacteriology · 2024Article
- Evidence for a compact σiScience · 2024Article
- RpoS and the bacterial general stress response.Microbiology and molecular biology reviews : MMBR · 2024Review
- Coordination of apicoplast transcription in a malaria parasite by internal and host cues.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Diverse and unified mechanisms of transcription initiation in bacteria.Nature reviews. Microbiology · 2021Review
- Article
- c-di-GMP Arms an Anti-σ to Control Progression of Multicellular Differentiation in Streptomyces.Molecular cell · 2020Article
- Alternative σI/anti-σI factors represent a unique form of bacterial σ/anti-σ complex.Nucleic acids research · 2019Article
- Diversity, versatility and complexity of bacterial gene regulation mechanisms: opportunities and drawbacks for applications in synthetic biology.FEMS microbiology reviews · 2019Review
- Coordinated Regulation of Rsd and RMF for Simultaneous Hibernation of Transcription Apparatus and Translation Machinery in Stationary-PhaseFrontiers in genetics · 2019Review
- The crystal structure of the RsbN-σBldN complex from Streptomyces venezuelae defines a new structural class of anti-σ factor.Nucleic acids research · 2018Article
- Linking glucose metabolism to the stringent response through the PTS.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function and Distribution.Biomolecules · 2015Review
- Structural biology of bacterial RNA polymerase.Biomolecules · 2015Review
- The TFE-induced transient native-like structure of the intrinsically disordered σ₄⁷⁰ domain of Escherichia coli RNA polymerase.European biophysics journal : EBJ · 2014Article
- HPr antagonizes the anti-σ70 activity of Rsd in Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Phage T7 Gp2 inhibition of Escherichia coli RNA polymerase involves misappropriation of σ70 domain 1.1.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Anti-Sigma Factors in E. coli: Common Regulatory Mechanisms Controlling Sigma Factors Availability.Current genomics · 2013Article
- Mycobacterium tuberculosis RsdA provides a conformational rationale for selective regulation of σ-factor activity by proteolysis.Nucleic acids research · 2013Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The Escherichia coli Rsd protein binds tightly and specifically to the RNA polymerase (RNAP) sigma(70) factor. Rsd plays a role in alternative sigma factor-dependent transcription by biasing the competition between sigma(70) and alternative sigma factors for the available core RNAP. Here, we determined the 2.6 A-resolution X-ray crystal structure of Rsd bound to sigma(70) domain 4 (sigma(70)(4)), the primary determinant for Rsd binding within sigma(70). The structure reveals that Rsd binding interferes with the two primary functions of sigma(70)(4), core RNAP binding and promoter -35 element binding. Interestingly, the most highly conserved Rsd residues form a network of interactions through the middle of the Rsd structure that connect the sigma(70)(4)-binding surface with three cavities exposed on distant surfaces of Rsd, suggesting functional coupling between sigma(70)(4) binding and other binding surfaces of Rsd, either for other proteins or for as yet unknown small molecule effectors. These results provide a structural basis for understanding the role of Rsd, as well as its ortholog, AlgQ, a positive regulator of Pseudomonas aeruginosa virulence, in transcription regulation.
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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.