ArticleJournal of bacteriology2013
Characterization of a novel RNA polymerase mutant that alters DksA activity.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Reciprocal cross-feeding between bacteria can limit the emergence of metabolic dependencies.Applied and environmental microbiology · 2026Article
- DksA-RNA polymerase interactions support new origin formation and DNA repair in Escherichia coli.Molecular microbiology · 2019Article
- TraR directly regulates transcription initiation by mimicking the combined effects of the global regulators DksA and ppGpp.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- ppGpp Binding to a Site at the RNAP-DksA Interface Accounts for Its Dramatic Effects on Transcription Initiation during the Stringent Response.Molecular cell · 2016Article
- DksA regulates RNA polymerase in Escherichia coli through a network of interactions in the secondary channel that includes Sequence Insertion 1.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- DksA involvement in transcription fidelity buffers stochastic epigenetic change.Nucleic acids research · 2015Article
- Regulation of transcription elongation and termination.Biomolecules · 2015Review
- Article
- Analysis of two domains with novel RNA-processing activities throws light on the complex evolution of ribosomal RNA biogenesis.Frontiers in genetics · 2014Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The auxiliary factor DksA is a global transcription regulator and, with the help of ppGpp, controls the nutritional stress response in Escherichia coli. Although the consequences of its modulation of RNA polymerase (RNAP) are becoming better explained, it is still not fully understood how the two proteins interact. We employed a series of genetic suppressor selections to find residues in RNAP that alter its sensitivity to DksA. Our approach allowed us to identify and genetically characterize in vivo three single amino acid substitutions: β' E677G, β V146F, and β G534D. We demonstrate that the mutation β' E677G affects the activity of both DksA and its homolog, TraR, but does not affect the action of other secondary interactors, such as GreA or GreB. Our mutants provide insight into how different auxiliary transcription factors interact with RNAP and contribute to our understanding of how different stages of transcription are regulated through the secondary channel of RNAP in vivo.
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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.