Structure of the DP1–DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases
|Author(s)||Raia Pierre1, 2, Carroni Marta3, Henry Etienne5, Pehau-Arnaudet Gerard1, 2, Brule Sebastien1, 2, Beguin Pierre1, Henneke Ghislaine4, Lindahl Erik3, Delarue Marc1, 2, Sauguet Ludovic1, 2|
|Affiliation(s)||1 : Pasteur Inst, Unit Struct Dynam Macromol, Paris, France.
2 : CNRS, UMR 3528, Paris, France.
3 : Stockholm Univ, Dept Biochem & Biophys, Sci Life Lab, Stockholm, Sweden.
4 : Univ Brest, CNRS, IFREMER, Lab Microbiol Environm Extremes, Plouzane, France.
|Source||Plos Biology (1545-7885) (Public Library Science), 2019-01 , Vol. 17 , N. 1 , P. e3000122 (28p.)|
|WOS© Times Cited||24|
PolD is an archaeal replicative DNA polymerase (DNAP) made of a proofreading exonuclease subunit (DP1) and a larger polymerase catalytic subunit (DP2). Recently, we reported the individual crystal structures of the DP1 and DP2 catalytic cores, thereby revealing that PolD is an atypical DNAP that has all functional properties of a replicative DNAP but with the catalytic core of an RNA polymerase (RNAP). We now report the DNA-bound cryo–electron microscopy (cryo-EM) structure of the heterodimeric DP1–DP2 PolD complex from Pyrococcus abyssi, revealing a unique DNA-binding site. Comparison of PolD and RNAPs extends their structural similarities and brings to light the minimal catalytic core shared by all cellular transcriptases. Finally, elucidating the structure of the PolD DP1–DP2 interface, which is conserved in all eukaryotic replicative DNAPs, clarifies their evolutionary relationships with PolD and sheds light on the domain acquisition and exchange mechanism that occurred during the evolution of the eukaryotic replisome.