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Volume 272, Number 25, Issue of June 20, 1997 pp. 15914-15919
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

The RNA Polymerase  Subunit Carboxyl-terminal Domain Is Required for Both Basal and Activated Transcription from the alkA Promoter

(Received for publication, February 25, 1997, and in revised form, April 16, 1997)

Paolo Landini , Tamas Gaal ^§ , Wilma Ross ^§ and Michael R. Volkert

From the  Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, Massachusetts 01655 and the ^§ Department of Bacteriology, University of Wisconsin, Madison, Wisconsin 53706

Expression of the Escherichia coli adaptive response genes (ada, aidB, and alkA) is regulated by the transcriptional activator, Ada. However, the interactions of RNA polymerase and Ada with these promoters differ. In this report we characterize the interactions of Ada, methylated Ada (^meAda), and RNA polymerase at the alkA promoter and contrast these interactions with those characterized previously for the ada and aidB promoters. At the alkA promoter, we do not detect the RNA polymerase  subunit-mediated binary complex detected at the ada and aidB promoters. In the presence of either of these two activators, RNA polymerase protects the alkA core promoter, including the elements at 35 and 10, and is more efficient in transcription initiation in vitro. RNA polymerase holoenzyme containing the  subunit mutation R265A is severely impaired in Ada-independent basal alkA transcription, shows no activation by Ada or ^meAda, and fails to bind the alkA promoter in vitro. Binding of the purified wild type  subunit to alkA was not detected, but a complex of promoter DNA, Ada or ^meAda, and  was observed in gel shift assays. These observations suggest that both forms of Ada protein activate alkA transcription by enhancing RNA polymerase holoenzyme and  subunit binding.

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