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The archaeal RNA polymerase (RNAP) shares structural similarities with eukaryotic RNAP II but requires a reduced subset of general transcription factors for promoter-dependent initiation. To deepen our knowledge of cellular transcription, we have determined the structure of the 13-subunit DNA-directed RNAP from Sulfolobus shibatae at 3.35 Å resolution. The structure contains the full complement of subunits, including RpoG/Rpb8 and the equivalent of the clamp-head and jaw domains of the eukaryotic Rpb1. Furthermore, we have identified subunit Rpo13, an RNAP component in the order Sulfolobales, which contains a helix-turn-helix motif that interacts with the RpoH/Rpb5 and RpoA'/Rpb1 subunits. Its location and topology suggest a role in the formation of the transcription bubble.

Original publication

DOI

10.1371/journal.pbio.1000102

Type

Journal article

Journal

PLoS Biol

Publication Date

05/2009

Volume

7

Keywords

Amino Acid Sequence, Archaeal Proteins, Crystallography, X-Ray, DNA-Directed RNA Polymerases, Evolution, Molecular, Models, Molecular, Molecular Sequence Data, Protein Subunits, RNA, Archaeal, Sulfolobus, Transcription, Genetic