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Journal of Bacteriology, September 2003, p. 5148-5157, Vol. 185, No. 17
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.17.5148-5157.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Cyclic AMP Receptor Protein-Dependent Activation of the Escherichia coli acsP2 Promoter by a Synergistic Class III Mechanism

Christine M. Beatty,1 Douglas F. Browning,1,2 Stephen J. W. Busby,2 and Alan J. Wolfe1*

Department of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, Maywood, Illinois 60153,1 School of Biosciences, University of Birmingham, Birmingham B15 2TT, United Kingdom2

Received 12 February 2003/ Accepted 16 June 2003

The cyclic AMP receptor protein (CRP) activates transcription of the Escherichia coli acs gene, which encodes an acetate-scavenging enzyme required for fitness during periods of carbon starvation. Two promoters direct transcription of acs, the distal acsP1 and the proximal acsP2. In this study, we demonstrated that acsP2 can function as the major promoter and showed by in vitro studies that CRP facilitates transcription by "focusing" RNA polymerase to acsP2. We proposed that CRP activates transcription from acsP2 by a synergistic class III mechanism. Consistent with this proposal, we showed that CRP binds two sites, CRP I and CRP II. Induction of acs expression absolutely required CRP I, while optimal expression required both CRP I and CRP II. The locations of these DNA sites for CRP (centered at positions -69.5 and -122.5, respectively) suggest that CRP interacts with RNA polymerase through class I interactions. In support of this hypothesis, we demonstrated that acs transcription requires the surfaces of CRP and the C-terminal domain of the {alpha} subunit of RNA polymerase holoenzyme ({alpha}-CTD), which is known to participate in class I interactions: activating region 1 of CRP and the 287, 265, and 261 determinants of the {alpha}-CTD. Other surface-exposed residues in the {alpha}-CTD contributed to acs transcription, suggesting that the {alpha}-CTD may interact with at least one protein other than CRP.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL 60153. Phone: (708) 216-5814. Fax: (708) 216-9574. E-mail: awolfe{at}lumc.edu.

Journal of Bacteriology, September 2003, p. 5148-5157, Vol. 185, No. 17
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.17.5148-5157.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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