FN Archimer Export Format
PT J
TI Structural basis for the increased processivity of D- family DNA polymerases in complex with PCNA
BT 
AF MADRU, Clément
   HENNEKE, Ghislaine
   RAIA, Pierre
   HUGONNEAU-BEAUFET, Inès
   PEHAU-ARNAUDET, Gérard
   ENGLAND, Patrick
   LINDAHL, Erik
   DELARUE, Marc
   CARRONI, Marta
   SAUGUET, Ludovic
AS 1:1;2:2;3:1,3;4:1;5:4;6:5;7:6,7;8:1;9:6;10:1;
FF 1:;2:PDG-REM-EEP-LMEE;3:;4:;5:;6:;7:;8:;9:;10:;
C1 Unit of Structural Dynamics of Macromolecules, Institut Pasteur and CNRS UMR 3528, Paris, France
   CNRS, Ifremer, Université de Brest, Laboratoire de Microbiologie des Environnements Extrêmes, Plouzané, France
   Sorbonne Université, École Doctorale Complexité du Vivant (ED515), Paris, France
   Utech UBI, Institut Pasteur, CNRS UMR 3528, Paris, France
   Molecular Biophysics Platform, C2RT, Institut Pasteur, CNRS UMR 3528, Paris, France
   Department of Biochemistry and Biophysics, Science for Life Laboratory, Stockholm University, Stockholm, Sweden
   Department of Applied Physics, KTH Royal Institute of Technology, Stockholm, Sweden
C2 INST PASTEUR, FRANCE
   IFREMER, FRANCE
   UNIV SORBONNE, FRANCE
   INST PASTEUR, FRANCE
   INST PASTEUR, FRANCE
   UNIV STOCKHOLM, SWEDEN
   KTH, SWEDEN
SI BREST
SE PDG-REM-EEP-LMEE
UM BEEP-LM2E
IN WOS Ifremer UMR
   DOAJ
   copubli-france
   copubli-europe
   copubli-univ-france
IF 14.919
TC 27
UR https://archimer.ifremer.fr/doc/00620/73180/72367.pdf
   https://archimer.ifremer.fr/doc/00620/73180/72374.pdf
   https://archimer.ifremer.fr/doc/00620/73180/72380.pdf
   https://archimer.ifremer.fr/doc/00620/73180/72381.pdf
   https://archimer.ifremer.fr/doc/00620/73180/72382.pdf
   https://archimer.ifremer.fr/doc/00620/73180/72383.pdf
   https://archimer.ifremer.fr/doc/00620/73180/72384.part
   https://archimer.ifremer.fr/doc/00620/73180/72386.xlsx
LA English
DT Article
AB Replicative DNA polymerases (DNAPs) have evolved the ability to copy the genome with high processivity and fidelity. In Eukarya and Archaea, the processivity of replicative DNAPs is greatly enhanced by its binding to the proliferative cell nuclear antigen (PCNA) that encircles the DNA. We determined the cryo-EM structure of the DNA-bound PolD–PCNA complex from Pyrococcus abyssi at 3.77 Å. Using an integrative structural biology approach — combining cryo-EM, X-ray crystallography, protein–protein interaction measurements, and activity assays — we describe the molecular basis for the interaction and cooperativity between a replicative DNAP and PCNA. PolD recruits PCNA via a complex mechanism, which requires two different PIP-boxes. We infer that the second PIP-box, which is shared with the eukaryotic Polα replicative DNAP, plays a dual role in binding either PCNA or primase, and could be a master switch between an initiation and a processive phase during replication. 
PY 2020
PD MAR
SO Nature Communications
SN 2041-1723
PU Nature Publishing Group
VL 11
IS 1
UT 000522437900007
DI 10.1038/s41467-020-15392-9
ID 73180
ER

EF