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The X-ray crystal structure of the euryarchaeal RNA polymerase in an open-clamp configuration

2014; Nature Portfolio; Volume: 5; Issue: 1 Linguagem: Inglês

10.1038/ncomms6132

2041-1723

Sung‐Hoon Jun, Akira Hirata, Tamotsu Kanai, Thomas J. Santangelo, Tadayuki Imanaka, Katsuhiko Murakami,

RNA Research and Splicing

The archaeal transcription apparatus is closely related to the eukaryotic RNA polymerase II (Pol II) system. Archaeal RNA polymerase (RNAP) and Pol II evolved from a common ancestral structure and the euryarchaeal RNAP is the simplest member of the extant archaeal–eukaryotic RNAP family. Here we report the first crystal structure of euryarchaeal RNAP from Thermococcus kodakarensis (Tko). This structure reveals that the clamp domain is able to swing away from the main body of RNAP in the presence of the Rpo4/Rpo7 stalk by coordinated movements of these domains. More detailed structure–function analysis of yeast Pol II and Tko RNAP identifies structural additions to Pol II that correspond to the binding sites of Pol II-specific general transcription factors including TFIIF, TFIIH and Mediator. Such comparisons provide a framework for dissecting interactions between RNAP and these factors during formation of the pre-initiation complex. Archaeal and eukaryotic RNA polymerases (RNAP) have conserved functional and structural similarities. Here, Jun et al.solve the first structure of a euryarchaeal RNAP in the open clamp conformation and identify insertions that may have evolved in eukaryotic Pol II to bind unique transcription factors.