FANCI binds branched DNA and is monoubiquitinated by UBE2T-FANCL

J Biol Chem. 2009 Aug 28;284(35):23182-6. doi: 10.1074/jbc.C109.038075. Epub 2009 Jul 8.

Abstract

FANCI is integral to the Fanconi anemia (FA) pathway of DNA damage repair. Upon the occurrence of DNA damage, FANCI becomes monoubiquitinated on Lys-523 and relocalizes to chromatin, where it functions with monoubiquitinated FANCD2 to facilitate DNA repair. We show that FANCI and its C-terminal fragment possess a DNA binding activity that prefers branched structures. We also demonstrate that FANCI can be ubiquitinated on Lys-523 by the UBE2T-FANCL pair in vitro. These findings should facilitate future efforts directed at elucidating molecular aspects of the FA pathway.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Cell Line
  • DNA / chemistry
  • DNA / genetics
  • DNA / metabolism*
  • DNA Repair
  • Fanconi Anemia Complementation Group L Protein / genetics
  • Fanconi Anemia Complementation Group L Protein / metabolism*
  • Fanconi Anemia Complementation Group Proteins / chemistry
  • Fanconi Anemia Complementation Group Proteins / genetics
  • Fanconi Anemia Complementation Group Proteins / metabolism*
  • Humans
  • Protein Binding
  • Protein Structure, Tertiary
  • Ubiquitin / metabolism
  • Ubiquitin-Conjugating Enzymes / genetics
  • Ubiquitin-Conjugating Enzymes / metabolism*
  • Ubiquitination

Substances

  • FANCI protein, human
  • Fanconi Anemia Complementation Group Proteins
  • Ubiquitin
  • DNA
  • UBE2T protein, human
  • Ubiquitin-Conjugating Enzymes
  • Fanconi Anemia Complementation Group L Protein