FANCI binds branched DNA and is monoubiquitinated by UBE2T-FANCL.
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.
Longerich
Simonne
S
Department of Molecular Biophysics, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
San Filippo
Joseph
J
Liu
Dongqing
D
Sung
Patrick
P
D000818:Animals; D002460:Cell Line; D004247:DNA / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004260:DNA Repair; D052240:Fanconi Anemia Complementation Group L Protein / Q000235:genetics / Q000378:metabolism*; D051856:Fanconi Anemia Complementation Group Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D025801:Ubiquitin / Q000378:metabolism; D044763:Ubiquitin-Conjugating Enzymes / Q000235:genetics / Q000378:metabolism*; D054875:Ubiquitination
C519921:FANCI protein, human; D051856:Fanconi Anemia Complementation Group Proteins; D025801:Ubiquitin; D004247:DNA; C513404:UBE2T protein, human; D044763:Ubiquitin-Conjugating Enzymes; D052240:Fanconi Anemia Complementation Group L Protein