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TitleCryo-EM structure of the Rev1-Polζ holocomplex reveals the mechanism of their cooperativity in translesion DNA synthesis.
Journal, issue, pagesNat Struct Mol Biol, Year 2024
Publish dateMay 8, 2024
AuthorsRadhika Malik / Robert E Johnson / Iban Ubarretxena-Belandia / Louise Prakash / Satya Prakash / Aneel K Aggarwal /
PubMed AbstractRev1-Polζ-dependent translesion synthesis (TLS) of DNA is crucial for maintaining genome integrity. To elucidate the mechanism by which the two polymerases cooperate in TLS, we determined the ...Rev1-Polζ-dependent translesion synthesis (TLS) of DNA is crucial for maintaining genome integrity. To elucidate the mechanism by which the two polymerases cooperate in TLS, we determined the cryogenic electron microscopic structure of the Saccharomyces cerevisiae Rev1-Polζ holocomplex in the act of DNA synthesis (3.53 Å). We discovered that a composite N-helix-BRCT module in Rev1 is the keystone of Rev1-Polζ cooperativity, interacting directly with the DNA template-primer and with the Rev3 catalytic subunit of Polζ. The module is positioned akin to the polymerase-associated domain in Y-family TLS polymerases and is set ideally to interact with PCNA. We delineate the full extent of interactions that the carboxy-terminal domain of Rev1 makes with Polζ and identify potential new druggable sites to suppress chemoresistance from first-line chemotherapeutics. Collectively, our results provide fundamental new insights into the mechanism of cooperativity between Rev1 and Polζ in TLS.
External linksNat Struct Mol Biol / PubMed:38720088
MethodsEM (single particle)
Resolution2.85 - 3.53 Å
Structure data

41371

8tlq

EMDB-41371, PDB-8tlq:
Cryo-EM structure of the Rev1-Polzeta-DNA-dCTP complex
Method: EM (single particle) / Resolution: 3.53 Å

41372

8tlt

EMDB-41372, PDB-8tlt:
Cryo-EM structure of Rev1(deltaN)-Polzeta-DNA-dCTP complex
Method: EM (single particle) / Resolution: 2.85 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-DCP:
2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE / Deoxycytidine triphosphate

ChemComp-SF4:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

ChemComp-HOH:
WATER / Water

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • dna molecule (others)
  • synthetic construct (others)
KeywordsDNA BINDING PROTEIN/DNA / DNA repair / DNA replication / translesion DNA synthesis / DNA polymerase / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex

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