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Helicobacter pylori FlgR Is an Enhancer-Independent Activator of σ(54)-RNA Polymerase Holoenzyme

By Priyanka Brahmachary, Mona G. Dashti, Jonathan W. Olson and Timothy R. Hoover


Helicobacter pylori FlgR activates transcription with σ(54)-RNA polymerase holoenzyme (σ(54)-holoenzyme) from at least five flagellar operons. Activators of σ(54)-holoenzyme generally bind enhancer sequences located >70 bp upstream of the promoter and contact σ(54)-holoenzyme bound at the promoter through DNA looping to activate transcription. H. pylori FlgR lacks the carboxy-terminal DNA-binding domain present in most σ(54)-dependent activators. As little as 42 bp of DNA upstream of the flaB promoter and 26 bp of DNA sequence downstream of the transcriptional start site were sufficient for efficient FlgR-mediated expression from a flaB′-′xylE reporter gene in H. pylori, indicating that FlgR does not use an enhancer to activate transcription. Other examples of σ(54)-dependent activators that lack a DNA-binding domain include Chlamydia trachomatis CtcC and activators from the other Chlamydia spp. whose genomes have been sequenced. FlgR from Helicobacter hepaticus and Campylobacter jejuni, which are closely related to H. pylori, appear to have carboxy-terminal DNA-binding domains, suggesting that the loss of the DNA-binding domain from H. pylori FlgR occurred after the divergence of these bacterial species. Removal of the amino-terminal regulatory domain of FlgR resulted in a constitutively active form of the protein that activated transcription from σ(54)-dependent genes in Escherichia coli. The truncated FlgR protein also activated transcription with E. coli σ(54)-holoenzyme in an in vitro transcription assay

Topics: Gene Regulation
Publisher: American Society for Microbiology
Year: 2004
DOI identifier: 10.1128/JB.186.14.4535-4542.2004
OAI identifier:
Provided by: PubMed Central
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