ArticleJournal of bacteriology2008
Differential mechanisms of binding of anti-sigma factors Escherichia coli Rsd and bacteriophage T4 AsiA to E. coli RNA polymerase lead to diverse physiological consequences.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 32 citations in OpenAlex.
- RNAP Promoter Search and Transcription Kinetics in LiveThe journal of physical chemistry. B · 2023Article
- Systemic Expression, Purification, and Initial Structural Characterization of Bacteriophage T4 Proteins Without Known Structure Homologs.Frontiers in microbiology · 2021Article
- Spatial organization of RNA polymerase and its relationship with transcription inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Regulation of Global Transcription inG3 (Bethesda, Md.) · 2018Article
- A model for sigma factor competition in bacterial cells.PLoS computational biology · 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
- Inactivation of the bacterial RNA polymerase due to acquisition of secondary structure by the ω subunit.The Journal of biological chemistry · 2013Article
- Evidence for sigma factor competition in the regulation of alginate production by Pseudomonas aeruginosa.PloS one · 2013Article
- The E. coli anti-sigma factor Rsd: studies on the specificity and regulation of its expression.PloS one · 2011Article
- In vivo transcription dynamics of the galactose operon: a study on the promoter transition from P1 to P2 at onset of stationary phase.PloS one · 2011Article
- Genetically engineered virulent phage banks in the detection and control of emergent pathogenic bacteria.Biosecurity and bioterrorism : biodefense strategy, practice, and science · 2010Article
- Structural and biochemical bases for the redox sensitivity of Mycobacterium tuberculosis RslA.Journal of molecular biology · 2010Article
- Inhibition of transcription in Staphylococcus aureus by a primary sigma factor-binding polypeptide from phage G1.Journal of bacteriology · 2009Article
- Rsd family proteins make simultaneous interactions with regions 2 and 4 of the primary sigma factor.Molecular microbiology · 2008Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Anti-sigma factors Escherichia coli Rsd and bacteriophage T4 AsiA bind to the essential housekeeping sigma factor, sigma(70), of E. coli. Though both factors are known to interact with the C-terminal region of sigma(70), the physiological consequences of these interactions are very different. This study was undertaken for the purpose of deciphering the mechanisms by which E. coli Rsd and bacteriophage T4 AsiA inhibit or modulate the activity of E. coli RNA polymerase, which leads to the inhibition of E. coli cell growth to different amounts. It was found that AsiA is the more potent inhibitor of in vivo transcription and thus causes higher inhibition of E. coli cell growth. Measurements of affinity constants by surface plasmon resonance experiments showed that Rsd and AsiA bind to sigma(70) with similar affinity. Data obtained from in vivo and in vitro binding experiments clearly demonstrated that the major difference between AsiA and Rsd is the ability of AsiA to form a stable ternary complex with RNA polymerase. The binding patterns of AsiA and Rsd with sigma(70) studied by using the yeast two-hybrid system revealed that region 4 of sigma(70) is involved in binding to both of these anti-sigma factors; however, Rsd interacts with other regions of sigma(70) as well. Taken together, these results suggest that the higher inhibition of E. coli growth by AsiA expression is probably due to the ability of the AsiA protein to trap the holoenzyme RNA polymerase rather than its higher binding affinity to sigma(70).
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