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J. Bacteriol. doi:10.1128/JB.01502-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Characterization of ResDE-Dependent fnr Transcription in Bacillus subtilis

Department of Environmental and Biomolecular Systems, OGI School of Science and Engineering, Oregon Health and Science University, 20000 NW Walker Road, Beaverton, Oregon 97006

^* To whom correspondence should be addressed. Email: mnakano{at}ebs.ogi.edu.

	Abstract

The ResD-ResE signal transduction system is required for transcription of genes involved in aerobic and anaerobic respiration in Bacillus subtilis. Phosphorylated ResD (ResDP) interacts with target DNA to activate transcription. A strong sequence similarity was detected in promoter regions of some ResD-controlled genes including fnr and resA. Single base substitutions of the fnr and resA promoters were carried out to determine a ResD-binding sequence. DNase I footprinting analysis indicated that ResDP itself does not bind to fnr, but interaction of ResDP with the C-terminal domain of the subunit (CTD) of RNA polymerase (RNAP) facilitates cooperative binding of ResDP and RNAP, thereby increasing fnr transcription initiation. Consistent with this result, amino acid substitutions in CTD, such as Y263A, K267A, A269I, or N290A, sharply reduced fnr transcription in vivo and the K267A CTD protein, unlike the wild-type protein, did not increase ResDP binding to the fnr promoter. Amino acid residues of CTD required for ResD-dependent fnr transcription, with the exception of N290, which may interact with DNA, constitute a distinct surface, suggesting that these residues likely interact with ResDP.

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