FN Archimer Export Format
PT J
TI Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography
BT 
AF SAUGUET, Ludovic
   RAIA, Pierre
   HENNEKE, Ghislaine
   DELARUE, Marc
AS 1:1,2;2:1,2,3;3:4,5,6;4:1,2;
FF 1:;2:;3:PDG-REM-EEP-LMEE;4:;
C1 Inst Pasteur, Unit Struct Dynam Macromol, F-75015 Paris, France.
   CNRS, UMR 3528, F-75015 Paris, France.
   Univ Paris 06, F-75006 Paris, France.
   IFREMER, UMR 6197, Lab Microbiol Environm Extremes, F-29280 Plouzane, France.
   UBO, UMR 6197, Lab Microbiol Environm Extremes, F-29280 Plouzane, France.
   CNRS, UMR 6197, Lab Microbiol Environm Extremes, F-29280 Plouzane, France.
C2 INST PASTEUR, FRANCE
   CNRS, FRANCE
   UNIV PARIS 06, FRANCE
   IFREMER, FRANCE
   UBO, FRANCE
   CNRS, FRANCE
SI BREST
SE PDG-REM-EEP-LMEE
UM BEEP-LM2E
IN WOS Ifremer jusqu'en 2018
   DOAJ
   copubli-france
   copubli-univ-france
IF 12.124
TC 35
UR https://archimer.ifremer.fr/doc/00350/46144/45842.pdf
   https://archimer.ifremer.fr/doc/00350/46144/45843.pdf
LA English
DT Article
AB 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.
PY 2016
PD AUG
SO Nature Communications
SN 2041-1723
PU Nature Publishing Group
VL 7
IS 12227
UT 000381904100001
BP 1
EP 12
DI 10.1038/ncomms12227
ID 46144
ER

EF