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Volume 271, Number 35, Issue of August 30, 1996 pp. 21453-21461
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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RNA Polymerase Signals UvrAB Landing Sites

(Received for publication, January 17, 1996, and in revised form, June 7, 1996)

From the Department of Biochemistry, School of Hygiene and Public Health, The Johns Hopkins University, Baltimore, Maryland 21205

Transcription when coupled to nucleotide excision repair specifies the location in active genes where preferential DNA repair is to take place. During DNA damage-induced recruitment of RNA polymerase (RNAP), there is a physical association of the  subunit of Escherichia coli RNAP and the UvrA component of the repair apparatus (G. C. Lin and L. Grossman, submitted for publication). This molecular affinity is reflected in the ability of the RNAP to increase, in a promoter-dependent manner, DNA supercoiling by the UvrAB complex. In the presence of the RNAP, the UvrAB complex is able to bind to promoter regions and to translocate in a 5 to 3 direction along the non-transcribed strand. As a consequence of this helicase-catalyzed translocation, preferential incision of DNA damaged sites occurs downstream on the transcribed strand. Because of the helicase directionality, the initial binding of the UvrAB complex to the transcribed strand would inevitably lead to its collision with the RNAP. These results imply that the RNAP-induced DNA structure in the vicinity of the transcription start site signals a landing or entry site for the UvrAB complex on DNA.

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This article has been cited by other articles:

				O. I. Kovalsky, L. Grossman, and B. Ahn The Topodynamics of Incision of UV-irradiated Covalently Closed DNA by the Escherichia coli Uvr(A)BC Endonuclease J. Biol. Chem., December 27, 1996; 271(52): 33236 - 33241. [Abstract] [Full Text] [PDF]

				B. Ahn and L. Grossman The Binding of UvrAB Proteins to Bubble and Loop Regions in Duplex DNA J. Biol. Chem., August 30, 1996; 271(35): 21462 - 21470. [Abstract] [Full Text] [PDF]