Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography

Type Article
Date 2016-08
Language English
Author(s) Sauguet Ludovic1, 2, Raia Pierre1, 2, 3, Henneke GhislaineORCID4, 5, 6, Delarue Marc1, 2
Affiliation(s) 1 : Inst Pasteur, Unit Struct Dynam Macromol, F-75015 Paris, France.
2 : CNRS, UMR 3528, F-75015 Paris, France.
3 : Univ Paris 06, F-75006 Paris, France.
4 : IFREMER, UMR 6197, Lab Microbiol Environm Extremes, F-29280 Plouzane, France.
5 : UBO, UMR 6197, Lab Microbiol Environm Extremes, F-29280 Plouzane, France.
6 : CNRS, UMR 6197, Lab Microbiol Environm Extremes, F-29280 Plouzane, France.
Source Nature Communications (2041-1723) (Nature Publishing Group), 2016-08 , Vol. 7 , N. 12227 , P. 1-12
DOI 10.1038/ncomms12227
WOS© Times Cited 31
Abstract Archaeal replicative DNA polymerase D (PolD) constitute an atypical class of DNA polymerases made of a proofreading exonuclease subunit (DP1) and a larger polymerase catalytic subunit (DP2), both with unknown structures. We have determined the crystal structures of Pyrococcus abyssi DP1 and DP2 at 2.5 and 2.2 angstrom resolution, respectively, revealing a catalytic core strikingly different from all other known DNA polymerases (DNAPs). Rather, the PolD DP2 catalytic core has the same 'double-psi beta-barrel' architecture seen in the RNA polymerase (RNAP) superfamily, which includes multi-subunit transcriptases of all domains of life, homodimeric RNA-silencing pathway RNAPs and atypical viral RNAPs. This finding bridges together, in non-viral world, DNA transcription and DNA replication within the same protein superfamily. This study documents further the complex evolutionary history of the DNA replication apparatus in different domains of life and proposes a classification of all extant DNAPs.
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Supplementary Figures 1-10, and Supplementary References. 15 17 MB Open access
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