Studies of the Escherichia coli Rsd-sigma70 complex

Escherichia coli Rsd protein was previously identified on the basis of its binding to the RNA polymerase sigma(70) subunit. The Rsd-sigma(70) complex has been studied using different methods. Our data show that Rsd associates with sigma(70) to form a complex with a stoichiometry of 1:1. Alanine scan...

Full description

Saved in:
Bibliographic Details
Published in:Journal of molecular biology 2004-01, Vol.335 (3), p.685
Main Authors: Westblade, Lars F, Ilag, Leopold L, Powell, Andrew K, Kolb, Annie, Robinson, Carol V, Busby, Stephen J W
Format: Article
Language:English
Subjects:
Binding Sites
DNA-Directed RNA Polymerases - chemistry
DNA-Directed RNA Polymerases - genetics
DNA-Directed RNA Polymerases - metabolism
Electrophoresis, Polyacrylamide Gel
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - metabolism
Molecular Weight
Mutagenesis, Site-Directed
Protein Binding
Repressor Proteins - chemistry
Repressor Proteins - metabolism
Sigma Factor - chemistry
Sigma Factor - genetics
Sigma Factor - metabolism
Spectrometry, Mass, Electrospray Ionization
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Escherichia coli Rsd protein was previously identified on the basis of its binding to the RNA polymerase sigma(70) subunit. The Rsd-sigma(70) complex has been studied using different methods. Our data show that Rsd associates with sigma(70) to form a complex with a stoichiometry of 1:1. Alanine scanning and deletion mutagenesis were used to locate regions of sigma(70) that are required for the formation of the Rsd-sigma(70) complex.
ISSN:0022-2836