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Science 17 May 2002:
Vol. 296. no. 5571, pp. 1280 - 1284
DOI: 10.1126/science.1069594
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Research Articles

Structural Basis of Transcription Initiation: RNA Polymerase Holoenzyme at 4 Å Resolution

Katsuhiko S. Murakami, Shoko Masuda, Seth A. Darst*

The crystal structure of the initiating form of Thermus aquaticus RNA polymerase, containing core RNA polymerase (alpha 2beta beta 'omega ) and the promoter specificity sigma  subunit, has been determined at 4 angstrom resolution. Important structural features of the RNA polymerase and their roles in positioning sigma  within the initiation complex are delineated, as well as the role played by sigma  in modulating the opening of the RNA polymerase active-site channel. The two carboxyl-terminal domains of sigma  are separated by 45 angstroms on the surface of the RNA polymerase, but are linked by an extended loop. The loop winds near the RNA polymerase active site, where it may play a role in initiating nucleotide substrate binding, and out through the RNA exit channel. The advancing RNA transcript must displace the loop, leading to abortive initiation and ultimately to sigma  release.

The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
*   To whom correspondence should be addressed. E-mail: darst{at}rockefeller.edu

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