Structure of a T7 RNA polymerase elongation complex at 2.9 Å resolution

Tahir H. Tahirov, Dmitry Temiakov, Michael Anikin, Vsevolod Patlan, William T. McAllister, Dmitry G. Vassylyev () and Shigeyuki Yokoyama ()
Additional contact information
Tahir H. Tahirov: High Throughput Factory, RIKEN Harima Institute at SPring-8
Dmitry Temiakov: SUNY Health Science Center
Michael Anikin: SUNY Health Science Center
Vsevolod Patlan: Structurome Research Group, RIKEN Harima Institute at SPring-8
William T. McAllister: SUNY Health Science Center
Dmitry G. Vassylyev: Structurome Research Group, RIKEN Harima Institute at SPring-8
Shigeyuki Yokoyama: Structurome Research Group, RIKEN Harima Institute at SPring-8

Nature, 2002, vol. 420, issue 6911, 43-50

Abstract: Abstract The single-subunit bacteriophage T7 RNA polymerase carries out the transcription cycle in an identical manner to that of bacterial and eukaryotic multisubunit enzymes. Here we report the crystal structure of a T7 RNA polymerase elongation complex, which shows that incorporation of an 8-base-pair RNA–DNA hybrid into the active site of the enzyme induces a marked rearrangement of the amino-terminal domain. This rearrangement involves alternative folding of about 130 residues and a marked reorientation (about 130° rotation) of a stable core subdomain, resulting in a structure that provides elements required for stable transcription elongation. A wide opening on the enzyme surface that is probably an RNA exit pathway is formed, and the RNA–DNA hybrid is completely buried in a newly formed, deep protein cavity. Binding of 10 base pairs of downstream DNA is stabilized mostly by long-distance electrostatic interactions. The structure implies plausible mechanisms for the various phases of the transcription cycle, and reveals important structural similarities with the multisubunit RNA polymerases.

Date: 2002
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DOI: 10.1038/nature01129

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