FN Archimer Export Format
PT J
TI Structure of the DP1–DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases
BT 
AF RAIA, Pierre
   CARRONI, Marta
   HENRY, Etienne
   PEHAU-ARNAUDET, Gerard
   BRULE, Sebastien
   BEGUIN, Pierre
   HENNEKE, Ghislaine
   LINDAHL, Erik
   DELARUE, Marc
   SAUGUET, Ludovic
AS 1:1,2;2:3;3:5;4:1,2;5:1,2;6:1;7:4;8:3;9:1,2;10:1,2;
FF 1:;2:;3:;4:;5:;6:;7:PDG-REM-EEP-LMEE;8:;9:;10:;
C1 Pasteur Inst, Unit Struct Dynam Macromol, Paris, France.
   CNRS, UMR 3528, Paris, France.
   Stockholm Univ, Dept Biochem & Biophys, Sci Life Lab, Stockholm, Sweden.
   Univ Brest, CNRS, IFREMER, Lab Microbiol Environm Extremes, Plouzane, France.
C2 INST PASTEUR, FRANCE
   CNRS, FRANCE
   UNIV STOCKHOLM, SWEDEN
   IFREMER, FRANCE
   CNRS, FRANCE
SI BREST
SE PDG-REM-EEP-LMEE
UM BEEP-LM2E
IN WOS Ifremer UMR
   WOS Cotutelle UMR
   DOAJ
   copubli-france
   copubli-europe
IF 9.163
TC 27
UR https://archimer.ifremer.fr/doc/00477/58883/61420.pdf
   https://archimer.ifremer.fr/doc/00477/58883/61421.pdf
   https://archimer.ifremer.fr/doc/00477/58883/61422.pdf
   https://archimer.ifremer.fr/doc/00477/58883/61423.pdf
   https://archimer.ifremer.fr/doc/00477/58883/61424.pdf
   https://archimer.ifremer.fr/doc/00477/58883/61425.pdf
   https://archimer.ifremer.fr/doc/00477/58883/61426.pdf
   https://archimer.ifremer.fr/doc/00477/58883/61427.pdf
   https://archimer.ifremer.fr/doc/00477/58883/61428.pdf
   https://archimer.ifremer.fr/doc/00477/58883/61429.pdf
   https://archimer.ifremer.fr/doc/00477/58883/61430.pdf
   https://archimer.ifremer.fr/doc/00477/58883/61431.xlsx
LA English
DT Article
AB 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. 
PY 2019
PD JAN
SO Plos Biology
SN 1545-7885
PU Public Library Science
VL 17
IS 1
UT 000457596000026
DI 10.1371/journal.pbio.3000122
ID 58883
ER

EF