Unknown

Dataset Information

0

Rearrangement of the RNA polymerase subunit H and the lower jaw in archaeal elongation complexes.


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 DeltaH 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.

SUBMITTER: Grunberg S 

PROVIDER: S-EPMC2847245 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

Rearrangement of the RNA polymerase subunit H and the lower jaw in archaeal elongation complexes.

Grünberg Sebastian S   Reich Christoph C   Zeller Mirijam E ME   Bartlett Michael S MS   Thomm Michael M  

Nucleic acids research 20091229 6


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 DeltaH  ...[more]

Similar Datasets

| S-EPMC9795356 | biostudies-literature
| S-EPMC6589136 | biostudies-literature
| S-EPMC2754188 | biostudies-literature
| S-EPMC2806685 | biostudies-literature
| S-EPMC2680338 | biostudies-literature
| S-EPMC524387 | biostudies-literature
| S-EPMC2791892 | biostudies-literature
| S-EPMC2911337 | biostudies-literature
| S-EPMC1271760 | biostudies-literature
| S-EPMC1500975 | biostudies-literature