Identification and characterization of a heterotrimeric archaeal DNA polymerase holoenzyme

Jiangyu Yan, Thomas R. Beattie, Adriana L. Rojas, Kelly Schermerhorn, Tamzin Gristwood, Jonathan C. Trinidad, Sonja V. Albers, Pietro Roversi, Andrew F. Gardner, Nicola G. A. Abrescia () and Stephen D. Bell ()
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Jiangyu Yan: Indiana University
Thomas R. Beattie: Sir William Dunn School of Pathology, University of Oxford
Adriana L. Rojas: Structural Biology Unit, CIC bioGUNE, CIBERehd
Kelly Schermerhorn: New England Biolabs
Tamzin Gristwood: Sir William Dunn School of Pathology, University of Oxford
Jonathan C. Trinidad: Indiana University
Sonja V. Albers: Molecular Biology of Archaea, Institute of Biology II, Microbiology, University of Freiburg
Pietro Roversi: Structural Biology Unit, CIC bioGUNE, CIBERehd
Andrew F. Gardner: New England Biolabs
Nicola G. A. Abrescia: Structural Biology Unit, CIC bioGUNE, CIBERehd
Stephen D. Bell: Indiana University

Nature Communications, 2017, vol. 8, issue 1, 1-15

Abstract: Abstract Since their initial characterization over 30 years ago, it has been believed that the archaeal B-family DNA polymerases are single-subunit enzymes. This contrasts with the multi-subunit B-family replicative polymerases of eukaryotes. Here we reveal that the highly studied PolB1 from Sulfolobus solfataricus exists as a heterotrimeric complex in cell extracts. Two small subunits, PBP1 and PBP2, associate with distinct surfaces of the larger catalytic subunit and influence the enzymatic properties of the DNA polymerase. Thus, multi-subunit replicative DNA polymerase holoenzymes are present in all three domains of life. We reveal the architecture of the assembly by a combination of cross-linking coupled with mass spectrometry, X-ray crystallography and single-particle electron microscopy. The small subunits stabilize the holoenzyme assembly and the acidic tail of one small subunit mitigates the ability of the enzyme to perform strand-displacement synthesis, with important implications for lagging strand DNA synthesis.

Date: 2017
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DOI: 10.1038/ncomms15075

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