ArticleThe Journal of biological chemistry2013
Inactivation of the bacterial RNA polymerase due to acquisition of secondary structure by the ω subunit.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- The ω subunit stabilizes transcribing RNA polymerase to balance processivity and collision resolution.bioRxiv : the preprint server for biology · 2026Article
- Global analysis of protein degradation reveals instability of diverse regulators inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- A flow equilibrium model controlling cytoplasmic transition metal cation pools and preventing mis-metalation as exemplified for zinc homeostasis.Journal of bacteriology · 2025Review
- Article
- A non-native C-terminal extension of the β' subunit compromises RNA polymerase and Rho functions.Molecular microbiology · 2022Article
- Validation of Omega Subunit of RNA Polymerase as a Functional Entity.Biomolecules · 2020Review
- Unraveling the Role of Silent Mutation in the ω-Subunit ofACS omega · 2019Article
- Association of ω with the C-Terminal Region of the β' Subunit Is Essential for Assembly of RNA Polymerase in Mycobacterium tuberculosis.Journal of bacteriology · 2018Article
- Influence of Flexible "ω" on the Activity of E. coli RNA Polymerase: A Thermodynamic Analysis.Biophysical journal · 2017Article
- Bacterial RNA Polymerase-DNA Interaction-The Driving Force of Gene Expression and the Target for Drug Action.Frontiers in molecular biosciences · 2016Review
- Suppression of capsule expression in Δlon strains of Escherichia coli by two novel rpoB mutations in concert with HNS: possible role for DNA bending at rcsA promoter.MicrobiologyOpen · 2015Article
- Distinct pathways of RNA polymerase regulation by a phage-encoded factor.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The omega subunit of the RNA polymerase core directs transcription efficiency in cyanobacteria.Nucleic acids research · 2014Article
- The sabotage of the bacterial transcription machinery by a small bacteriophage protein.Bacteriophage · 2014Article
- Altered Distribution of RNA Polymerase Lacking the Omega Subunit within the Prophages along themSystemsArticle
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The widely conserved ω subunit encoded by rpoZ is the smallest subunit of Escherichia coli RNA polymerase (RNAP) but is dispensable for bacterial growth. Function of ω is known to be substituted by GroEL in ω-null strain, which thus does not exhibit a discernable phenotype. In this work, we report isolation of ω variants whose expression in vivo leads to a dominant lethal phenotype. Studies show that in contrast to ω, which is largely unstructured, ω mutants display substantial acquisition of secondary structure. By detailed study with one of the mutants, ω6 bearing N60D substitution, the mechanism of lethality has been deciphered. Biochemical analysis reveals that ω6 binds to β' subunit in vitro with greater affinity than that of ω. The reconstituted RNAP holoenzyme in the presence of ω6 in vitro is defective in transcription initiation. Formation of a faulty RNAP in the presence of mutant ω results in death of the cell. Furthermore, lethality of ω6 is relieved in cells expressing the rpoC2112 allele encoding β'2112, a variant β' bearing Y457S substitution, immediately adjacent to the β' catalytic center. Our results suggest that the enhanced ω6-β' interaction may perturb the plasticity of the RNAP active center, implicating a role for ω and its flexible state.
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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.