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TitleStructures of the human leading strand Polε-PCNA holoenzyme.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 7847, Year 2024
Publish dateSep 8, 2024
AuthorsQing He / Feng Wang / Nina Y Yao / Michael E O'Donnell / Huilin Li /
PubMed AbstractIn eukaryotes, the leading strand DNA is synthesized by Polε and the lagging strand by Polδ. These replicative polymerases have higher processivity when paired with the DNA clamp PCNA. While the ...In eukaryotes, the leading strand DNA is synthesized by Polε and the lagging strand by Polδ. These replicative polymerases have higher processivity when paired with the DNA clamp PCNA. While the structure of the yeast Polε catalytic domain has been determined, how Polε interacts with PCNA is unknown in any eukaryote, human or yeast. Here we report two cryo-EM structures of human Polε-PCNA-DNA complex, one in an incoming nucleotide bound state and the other in a nucleotide exchange state. The structures reveal an unexpected three-point interface between the Polε catalytic domain and PCNA, with the conserved PIP (PCNA interacting peptide)-motif, the unique P-domain, and the thumb domain each interacting with a different protomer of the PCNA trimer. We propose that the multi-point interface prevents other PIP-containing factors from recruiting to PCNA while PCNA functions with Polε. Comparison of the two states reveals that the finger domain pivots around the [4Fe-4S] cluster-containing tip of the P-domain to regulate nucleotide exchange and incoming nucleotide binding.
External linksNat Commun / PubMed:39245668 / PubMed Central
MethodsEM (single particle)
Resolution2.95 - 5.01 Å
Structure data

44357

9b8s

EMDB-44357, PDB-9b8s:
Human polymerase epsilon bound to PCNA and DNA in the nucleotide exchange state
Method: EM (single particle) / Resolution: 5.01 Å

44358

9b8t

EMDB-44358, PDB-9b8t:
Human polymerase epsilon bound to PCNA and DNA in the nucleotide bound state
Method: EM (single particle) / Resolution: 2.95 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-TTP:
THYMIDINE-5'-TRIPHOSPHATE

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
  • dna molecule (others)
KeywordsDNA Binding Protein/DNA / DNA polymerase / DNA / DNA Binding Protein-DNA complex

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