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

© The Author(s) 2009. Published by Oxford University Press on behalf of Nucleic Acids Research.

Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial 2.5 International License.

The article is available online: https://doi.org/10.1093/nar/gkp1190

Supplementary data is available online: 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

Share

COinS