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Nucleic Acids Research 2005 33(8):2629-2639; doi:10.1093/nar/gki570
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Published online 10 May 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

The highly conserved glutamic acid 791 of Rpb2 is involved in the binding of NTP and Mg(B) in the active center of human RNA polymerase II

Marie-France Langelier, Dania Baali, Vincent Trinh, Jack Greenblatt1, Jacques Archambault2 and Benoit Coulombe*

Laboratory of Gene Transcription, Institut de recherches cliniques de Montréal 110 avenue des Pins Ouest, Montréal, Québec, Canada H2W 1R7 1Banting and Best Department of Medical Research, University of Toronto Toronto, Ontario, Canada M5G 1L6 2Laboratory of Molecular Virology, Institut de recherches cliniques de Montréal 110 avenue des Pins Ouest, Montréal, Québec, Canada H2W 1R7

*To whom correspondence should be addressed. Tel: +1 514 987 5662; Fax: +1 514 987 5663; Email: benoit.coulombe{at}ircm.qc.ca

Received February 2, 2005. Revised April 21, 2005. Accepted April 21, 2005.

During transcription by RNA polymerase (RNAP) II, the incoming ribonucleoside triphosphate (NTP) enters the catalytic center in association with an Mg2+ ion, termed metal B [Mg(B)]. When bound to RNAP II, Mg(B) is coordinated by the ß and {gamma} phosphates of the NTP, Rpb1 residues D481 and D483 and Rpb2 residue D837. Rpb2 residue D837 is highly conserved across species. Notably, its neighboring residue, E836 (E791 in human RNAP II), is also highly conserved. To probe the role of E791 in transcription, we have affinity purified and characterized a human RNAP II mutant in which this residue was substituted for alanine. Our results indicate that the transcription activity of the Rpb2 E791A mutant is impaired at low NTP concentrations both in vitro and in vivo. They also revealed that both its NTP polymerization and transcript cleavage activities are decreased at low Mg concentrations. Because Rpb2 residue E791 appears to be located too far from the NTP–Mg(B) complex to make direct contact at either the entry (E) or addition (A) site, we propose alternative mechanisms by which this highly conserved residue participates in loading NTP–Mg(B) in the active site during transcription.


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Home page
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V. Trinh, M.-F. Langelier, J. Archambault, and B. Coulombe
Structural Perspective on Mutations Affecting the Function of Multisubunit RNA Polymerases
Microbiol. Mol. Biol. Rev., March 1, 2006; 70(1): 12 - 36.
[Abstract] [Full Text] [PDF]


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