Abstract:
: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.
journal_name
PLoS Bioljournal_title
PLoS biologyauthors
Raia P,Carroni M,Henry E,Pehau-Arnaudet G,Brûlé S,Béguin P,Henneke G,Lindahl E,Delarue M,Sauguet Ldoi
10.1371/journal.pbio.3000122subject
Has Abstractpub_date
2019-01-18 00:00:00pages
e3000122issue
1eissn
1544-9173issn
1545-7885pii
PBIOLOGY-D-18-00775journal_volume
17pub_type
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