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© Ludovic Sauguet, Institut Pasteur
Publication : Nature communications

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nature communications - 01 Jan 2016

Sauguet L, Raia P, Henneke G, Delarue M,

Link to Pubmed [PMID] – 27548043

Link to DOI – 10.1038/ncomms12227

Nat Commun 2016 ; 7(): 12227

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 Å 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 β-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.

https://pubmed.ncbi.nlm.nih.gov/27548043