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TitleStructural basis of FANCD2 deubiquitination by USP1-UAF1.
Journal, issue, pagesNat Struct Mol Biol, Vol. 28, Issue 4, Page 356-364, Year 2021
Publish dateApr 1, 2021
AuthorsMartin L Rennie / Connor Arkinson / Viduth K Chaugule / Rachel Toth / Helen Walden /
PubMed AbstractUbiquitin-specific protease 1 (USP1) acts together with the cofactor UAF1 during DNA repair processes to specifically remove monoubiquitin signals. One substrate of the USP1-UAF1 complex is the ...Ubiquitin-specific protease 1 (USP1) acts together with the cofactor UAF1 during DNA repair processes to specifically remove monoubiquitin signals. One substrate of the USP1-UAF1 complex is the monoubiquitinated FANCI-FANCD2 heterodimer, which is involved in the repair of DNA interstrand crosslinks via the Fanconi anemia pathway. Here we determine structures of human USP1-UAF1 with and without ubiquitin and bound to monoubiquitinated FANCI-FANCD2. The crystal structures of USP1-UAF1 reveal plasticity in USP1 and key differences to USP12-UAF1 and USP46-UAF1, two related proteases. A cryo-EM reconstruction of USP1-UAF1 in complex with monoubiquitinated FANCI-FANCD2 highlights a highly orchestrated deubiquitination process, with USP1-UAF1 driving conformational changes in the substrate. An extensive interface between UAF1 and FANCI, confirmed by mutagenesis and biochemical assays, provides a molecular explanation for the requirement of both proteins, despite neither being directly involved in catalysis. Overall, our data provide molecular details of USP1-UAF1 regulation and substrate recognition.
External linksNat Struct Mol Biol / PubMed:33795880
MethodsEM (single particle) / X-ray diffraction
Resolution3.2 - 3.7 Å
Structure data

11934

7ay1

EMDB-11934, PDB-7ay1:
Cryo-EM structure of USP1-UAF1 bound to mono-ubiquitinated FANCD2, and FANCI
Method: EM (single particle) / Resolution: 3.7 Å

PDB-7ay0:
Crystal structure of truncated USP1-UAF1
Method: X-RAY DIFFRACTION / Resolution: 3.6 Å

PDB-7ay2:
Crystal structure of truncated USP1-UAF1 reacted with ubiquitin-prg
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-AYE:
prop-2-en-1-amine / Allylamine

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsHYDROLASE / deubiquitination / specificity / DNA repair / Fanconi Anemia

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