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J. Bacteriol. doi:10.1128/JB.01599-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Affinity isolation and I-DIRT mass spectrometric analysis of the Escherichia coli O157:H7 Sakai RNA polymerase complex

School of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK; The Rockefeller University, New York, NY 10065, USA

^* To whom correspondence should be addressed. Email: D.lee{at}bham.ac.uk.

	Abstract

Bacteria contain a single multi-subunit RNA polymerase that is responsible for the synthesis of all RNA. Previous studies on the Escherichia coli K-12 laboratory strain had identified a group of effector proteins that interact directly with RNA polymerase to modulate the efficiency of transcription initiation, elongation or termination. Here we have used a rapid affinity isolation technique to isolate RNA polymerase from the pathogenic Escherichia coli O157:H7 Sakai strain. We analysed the RNA polymerase enzyme complex using mass spectrometry and identified associated proteins. Although Escherichia coli O157:H7 Sakai contains more than 1,600 genes not present in the K-12 strain, many of which are predicted to be involved in transcription regulation, all of the identified proteins in this study were coded on the ‘core’ Escherichia coli genome.