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TitleHuman polymerase θ helicase positions DNA microhomologies for double-strand break repair.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 6, Page 1061-1068, Year 2025
Publish dateFeb 28, 2025
AuthorsChristopher J Zerio / Yonghong Bai / Brian A Sosa-Alvarado / Timothy Guzi / Gabriel C Lander /
PubMed AbstractDNA double-strand breaks occur daily in all human cells and must be repaired with high fidelity to minimize genomic instability. Deficiencies in high-fidelity DNA repair by homologous recombination ...DNA double-strand breaks occur daily in all human cells and must be repaired with high fidelity to minimize genomic instability. Deficiencies in high-fidelity DNA repair by homologous recombination lead to dependence on DNA polymerase θ, which identifies DNA microhomologies in 3' single-stranded DNA overhangs and anneals them to initiate error-prone double-strand break repair. The resulting genomic instability is associated with numerous cancers, thereby making this polymerase an attractive therapeutic target. However, despite the biomedical importance of polymerase θ, the molecular details of how it initiates DNA break repair remain unclear. Here, we present cryo-electron microscopy structures of the polymerase θ helicase domain bound to microhomology-containing DNA, revealing DNA-induced rearrangements of the helicase that enable DNA repair. Our structures show that DNA-bound helicase dimers facilitate a microhomology search that positions 3' single-stranded DNA ends in proximity to align complementary bases and anneal DNA microhomology. We characterize the molecular determinants that enable the helicase domain of polymerase θ to identify and pair DNA microhomologies to initiate mutagenic DNA repair, thereby providing insight into potentially targetable interactions for therapeutic interventions.
External linksNat Struct Mol Biol / PubMed:40021738 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.6 Å
Structure data

44534

9bh6

EMDB-44534, PDB-9bh6:
Human DNA polymerase theta helicase domain tetramer in the apo form
Method: EM (single particle) / Resolution: 3.3 Å

44535

9bh7

EMDB-44535, PDB-9bh7:
Human DNA polymerase theta helicase domain dimer in the apo form
Method: EM (single particle) / Resolution: 3.5 Å

44536

9bh8

EMDB-44536, PDB-9bh8:
Human DNA polymerase theta helicase domain dimer bound to DNA in the microhomology searching conformation
Method: EM (single particle) / Resolution: 3.6 Å

44537

9bh9

EMDB-44537, PDB-9bh9:
Human DNA polymerase theta helicase domain dimer bound to DNA in the microhomology aligning conformation
Method: EM (single particle) / Resolution: 3.5 Å

44538

9bha

EMDB-44538, PDB-9bha:
Human DNA polymerase theta helicase domain dimer bound to DNA in the microhomology annealed conformation
Method: EM (single particle) / Resolution: 3.5 Å

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsDNA BINDING PROTEIN / DNA repair / TMEJ / MMEJ

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