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
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Research Support, N.I.H., Extramural
MeSH terms
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Animals
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Cell Line
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DNA / chemistry
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DNA / genetics
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DNA / metabolism*
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DNA Repair
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Fanconi Anemia Complementation Group L Protein / genetics
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Fanconi Anemia Complementation Group L Protein / metabolism*
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Fanconi Anemia Complementation Group Proteins / chemistry
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Fanconi Anemia Complementation Group Proteins / genetics
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Fanconi Anemia Complementation Group Proteins / metabolism*
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Humans
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Protein Binding
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Protein Structure, Tertiary
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Ubiquitin / metabolism
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Ubiquitin-Conjugating Enzymes / genetics
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Ubiquitin-Conjugating Enzymes / metabolism*
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Ubiquitination
Substances
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FANCI protein, human
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Fanconi Anemia Complementation Group Proteins
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Ubiquitin
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DNA
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UBE2T protein, human
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Ubiquitin-Conjugating Enzymes
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Fanconi Anemia Complementation Group L Protein