ArticleJournal of bacteriology2014
ε, a new subunit of RNA polymerase found in gram-positive bacteria.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 35 citations in OpenAlex.
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- A noncanonical RNA polymerase assembly pathway in Bacillus subtilis: α Dimer associates with either β or β' before forming the core enzyme.The Journal of biological chemistry · 2026Article
- Systematic modulation of bacterial resource allocation by perturbing RNA polymerase availability via synthetic transcriptional switches.Nucleic acids research · 2025Article
- How do bacteria tune transcription termination efficiency?Current opinion in microbiology · 2024Review
- Membrane platform protein PulF of themBio · 2024Article
- Article
- QSAR, Docking, and Molecular Dynamics Simulation Studies of Sigmacidins as Antimicrobials againstInternational journal of molecular sciences · 2022Article
- Multiple classes and isoforms of the RNA polymerase recycling motor protein HelD.MicrobiologyOpen · 2021Article
- Molecular Modeling the Proteins from theAntibiotics (Basel, Switzerland) · 2021Review
- Structural basis of transcription activation by the global regulator Spx.Nucleic acids research · 2021Article
- RNA polymerases from low G+C gram-positive bacteria.Transcription · 2021Review
- The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling.Nature communications · 2020Article
- Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD.Nature communications · 2020Article
- Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase.Nature communications · 2020Article
- The bacterial multidrug resistance regulator BmrR distorts promoter DNA to activate transcription.Nature communications · 2020Article
- Validation of Omega Subunit of RNA Polymerase as a Functional Entity.Biomolecules · 2020Review
- The torpedo effect in Bacillus subtilis: RNase J1 resolves stalled transcription complexes.The EMBO journal · 2020Article
- Solution structure of domain 1.1 of the σThe Journal of biological chemistry · 2017Article
- The ω Subunit Governs RNA Polymerase Stability and Transcriptional Specificity in Staphylococcus aureus.Journal of bacteriology · 2017Article
- Bacterial Transcription as a Target for Antibacterial Drug Development.Microbiology and molecular biology reviews : MMBR · 2016Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNA polymerase in bacteria is a multisubunit protein complex that is essential for gene expression. We have identified a new subunit of RNA polymerase present in the high-A+T Firmicutes phylum of Gram-positive bacteria and have named it ε. Previously ε had been identified as a small protein (ω1) that copurified with RNA polymerase. We have solved the structure of ε by X-ray crystallography and show that it is not an ω subunit. Rather, ε bears remarkable similarity to the Gp2 family of phage proteins involved in the inhibition of host cell transcription following infection. Deletion of ε shows no phenotype and has no effect on the transcriptional profile of the cell. Determination of the location of ε within the assembly of RNA polymerase core by single-particle analysis suggests that it binds toward the downstream side of the DNA binding cleft. Due to the structural similarity of ε with Gp2 and the fact they bind similar regions of RNA polymerase, we hypothesize that ε may serve a role in protection from phage infection.
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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.