Residues 137 and 153 of XylS influence contacts with the C-terminal domain of the RNA polymerase alpha subunit

R Ruiz; J L Ramos

doi:10.1006/bbrc.2001.5615

Residues 137 and 153 of XylS influence contacts with the C-terminal domain of the RNA polymerase alpha subunit

Biochem Biophys Res Commun. 2001 Sep 21;287(2):519-21. doi: 10.1006/bbrc.2001.5615.

Authors

R Ruiz¹, J L Ramos

Affiliation

¹ Department Biochemistry and Molecular and Cellular Biology of Plants, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas, Apartado de Correos 419, E-18008 Granada, Spain.

PMID: 11554759
DOI: 10.1006/bbrc.2001.5615

Abstract

XylS and XylS1 are transcriptional regulators that stimulate transcription from the Pm promoter for the meta-cleavage pathway operon for alkylbenzoate degradation. These regulators that differ in five amino acids interact with alpha-CTD domain of RNA polymerase. These interactions take place preferentially through residues 291 in XylS and 289 in XylS1. Substitution at position 137 and 153 in XylS influence the interactions with alpha-CTD because single and double mutants in these positions turned preferential interactions to residue 289.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins / genetics
Bacterial Proteins / metabolism*
DNA-Binding Proteins
DNA-Directed RNA Polymerases / chemistry
DNA-Directed RNA Polymerases / metabolism*
Escherichia coli
Mutation
Protein Structure, Tertiary
Pseudomonas / chemistry*
Pseudomonas / genetics
Trans-Activators / genetics
Trans-Activators / metabolism*

Substances

Bacterial Proteins
DNA-Binding Proteins
Trans-Activators
XylS protein, Pseudomonas putida
DNA-Directed RNA Polymerases
RNA polymerase alpha subunit