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TitleFANCD2-FANCI surveys DNA and recognizes double- to single-stranded junctions.
Journal, issue, pagesNature, Vol. 632, Issue 8027, Page 1165-1173, Year 2024
Publish dateJul 31, 2024
AuthorsPablo Alcón / Artur P Kaczmarczyk / Korak Kumar Ray / Themistoklis Liolios / Guillaume Guilbaud / Tamara Sijacki / Yichao Shen / Stephen H McLaughlin / Julian E Sale / Puck Knipscheer / David S Rueda / Lori A Passmore /
PubMed AbstractDNA crosslinks block DNA replication and are repaired by the Fanconi anaemia pathway. The FANCD2-FANCI (D2-I) protein complex is central to this process as it initiates repair by coordinating DNA ...DNA crosslinks block DNA replication and are repaired by the Fanconi anaemia pathway. The FANCD2-FANCI (D2-I) protein complex is central to this process as it initiates repair by coordinating DNA incisions around the lesion. However, D2-I is also known to have a more general role in DNA repair and in protecting stalled replication forks from unscheduled degradation. At present, it is unclear how DNA crosslinks are recognized and how D2-I functions in replication fork protection. Here, using single-molecule imaging, we show that D2-I is a sliding clamp that binds to and diffuses on double-stranded DNA. Notably, sliding D2-I stalls on encountering single-stranded-double-stranded (ss-ds) DNA junctions, structures that are generated when replication forks stall at DNA lesions. Using cryogenic electron microscopy, we determined structures of D2-I on DNA that show that stalled D2-I makes specific interactions with the ss-dsDNA junction that are distinct from those made by sliding D2-I. Thus, D2-I surveys dsDNA and, when it reaches an ssDNA gap, it specifically clamps onto ss-dsDNA junctions. Because ss-dsDNA junctions are found at stalled replication forks, D2-I can identify sites of DNA damage. Therefore, our data provide a unified molecular mechanism that reconciles the roles of D2-I in the recognition and protection of stalled replication forks in several DNA repair pathways.
External linksNature / PubMed:39085614 / PubMed Central
MethodsEM (single particle)
Resolution3.59 - 3.68 Å
Structure data

EMDB-50353: ss-dsDNA-FANCD2-FANCI complex
Method: EM (single particle) / Resolution: 3.59 Å

EMDB-50355: dsDNA-FANCD2-FANCI complex
Method: EM (single particle) / Resolution: 3.68 Å

Source
  • Gallus gallus (chicken)
  • synthetic construct (others)

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