Published In

Nucleic Acids Research

Document Type

Article

Publication Date

12-29-2009

Subjects

Transcription - Genetic, Archaeal proteins - Metabolism, Base sequence - DNA, Molecular Sequence Data

Abstract

The lower jaws of archaeal RNA polymerase and eukaryotic RNA polymerase II include orthologous subunits H and Rpb5, respectively. The tertiary structure of H is very similar to the structure of the C-terminal domain of Rpb5, and both subunits are proximal to downstream DNA in pre-initiation complexes. Analyses of reconstituted euryarchaeal polymerase lacking subunit H revealed that H is important for open complex formation and initial transcription. Eukaryotic Rpb5 rescues activity of the ΔH enzyme indicating a strong conservation of function for this subunit from archaea to eukaryotes. Photochemical cross-linking in elongation complexes revealed a striking structural rearrangement of RNA polymerase, bringing subunit H near the transcribed DNA strand one helical turn downstream of the active center, in contrast to the positioning observed in preinitiation complexes. The rearrangement of subunits H and A'' suggest a major conformational change in the archaeal RNAP lower jaw upon formation of the elongation complex.

Description

Copyright 2009 The Authors. Published by Oxford University Press in Nucleic Acids Research, 2010, Vol. 38, No. 6, an Open Access Journal.

Distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/ by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary data http://nar.oxfordjournals.org/content/suppl/2009/12/30/gkp1190.DC1

DOI

10.1093/nar/gkp1190

Persistent Identifier

http://archives.pdx.edu/ds/psu/10491

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