The transcriptional activator of the bfp operon in EPEC (PerA) interacts with the RNA polymerase alpha subunit
| Autor: | Jorge A. Girón, Sergio I Vázquez-Arellano, Abraham Medrano-López, Luis E. Romero-González, Ernesto Pérez-Rueda, Cristina Lara-Ochoa, Ygnacio Martínez-Laguna, Lilia Cedillo-Ramírez, Juan B Jaramillo-Rodríguez, José L. Puente, Fabiola González-Lara, J. Antonio Ibarra |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Operon Science 030106 microbiology Biology Microbiology Article Pera Enteropathogenic Escherichia coli 03 medical and health sciences chemistry.chemical_compound Bacterial genetics RNA polymerase Promoter Regions Genetic Gene Escherichia coli Infections Polymerase G alpha subunit Multidisciplinary Virulence Escherichia coli Proteins DNA-Directed RNA Polymerases biology.organism_classification Cell biology Repressor Proteins 030104 developmental biology chemistry Regulatory sequence biology.protein Medicine Microbial genetics Transcription Factors Locus of enterocyte effacement |
| Zdroj: | Scientific Reports, Vol 11, Iss 1, Pp 1-11 (2021) Scientific Reports |
| ISSN: | 2045-2322 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink