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Structure of the DP1-DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).ORCID iD: 0000-0002-7697-6427
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Number of Authors: 102019 (English)In: PLoS biology, ISSN 1544-9173, E-ISSN 1545-7885, Vol. 17, no 1, article id e3000122Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2019. Vol. 17, no 1, article id e3000122
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Biological Sciences
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URN: urn:nbn:se:su:diva-166628DOI: 10.1371/journal.pbio.3000122ISI: 000457596000026PubMedID: 30657780OAI: oai:DiVA.org:su-166628DiVA, id: diva2:1296783
Available from: 2019-03-18 Created: 2019-03-18 Last updated: 2019-03-18Bibliographically approved

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Raia, PierreCarroni, MartaBeguin, PierreLindahl, Erik
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