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School of Biosciences, University of Birmingham, Birmingham B15 2TT, United Kingdom,1 Nara Institute of Science and Technology, Nara 630-0101, Japan,2 The Rockefeller University, 1230 York Avenue, New York, New York 10021,3 Institut Pasteur, 25 rue du Dr Roux, F75724 Paris cedex 15, France4
Received 4 January 2007/ Accepted 19 February 2007
The Escherichia coli Rsd protein forms complexes with the RNA polymerase
70 factor, but its biological role is not understood. Transcriptome analysis shows that overexpression of Rsd causes increased expression from some promoters whose expression depends on the alternative
38 factor, and this was confirmed by experiments with lac fusions at selected promoters. The LP18 substitution in Rsd increases the Rsd-dependent stimulation of these promoter-lac fusions. Analysis with a bacterial two-hybrid system shows that the LP18 substitution in Rsd increases its interaction with
70. Our experiments support a model in which the role of Rsd is primarily to sequester
70, thereby increasing the levels of RNA polymerase containing the alternative
38 factor.
Published ahead of print on 9 March 2007.
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