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FANCI binds branched DNA and is monoubiquitinated by UBE2T-FANCL.

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.

SUBMITTER: Longerich S

PROVIDER: S-EPMC2749091 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature

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FANCI binds branched DNA and is monoubiquitinated by UBE2T-FANCL.

Longerich Simonne S San Filippo Joseph J Liu Dongqing D Sung Patrick P

The Journal of biological chemistry 20090708 35

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 ...[more]

PMID: 19589784

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FANCI protein binds to DNA and interacts with FANCD2 to recognize branched structures.

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