ArticleScientific reports2021
The transcriptional activator of the bfp operon in EPEC (PerA) interacts with the RNA polymerase alpha subunit.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Type IV pilin regulation: a transcriptional overview.Critical reviews in microbiology · 2026Review
- Regulation of dgcZ in EPEC E2348/69 and the effect of partially deleting its CZB domain on the type III secretion system.FEMS microbiology letters · 2026Article
- Interactions between the AraC/XylS-like transcriptional activator InvF of Salmonella Typhimurium, the RNA polymerase alpha subunit and the chaperone SicA.Scientific reports · 2024Article
- Article
- The Assembly of Flagella in EnteropathogenicInternational journal of molecular sciences · 2022Article
- The Transcription of Flagella of EnteropathogenicMicroorganisms · 2022Article
- High variation acrossGut microbesArticle
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enteropathogenic E. coli virulence genes are under the control of various regulators, one of which is PerA, an AraC/XylS-like regulator. PerA directly promotes its own expression and that of the bfp operon encoding the genes involved in the biogenesis of the bundle-forming pilus (BFP); it also activates PerC expression, which in turn stimulates locus of enterocyte effacement (LEE) activation through the LEE-encoded regulator Ler. Monomeric PerA directly binds to the per and bfp regulatory regions; however, it is not known whether interactions between PerA and the RNA polymerase (RNAP) are needed to activate gene transcription as has been observed for other AraC-like regulators. Results showed that PerA interacts with the alpha subunit of the RNAP polymerase and that it is necessary for the genetic and phenotypic expression of bfpA. Furthermore, an in silico analysis shows that PerA might be interacting with specific alpha subunit amino acids residues highlighting the direction of future experiments.
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Registered trials
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