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The FHA domain of aprataxin interacts with the C-terminal region of XRCC1.

http://www.ncbi.nlm.nih.gov/pubmed/15555565

Aprataxin (APTX) is the causative gene product for early-onset ataxia with ocular motor apraxia and hypoalbuminemia (EAOH/AOA1). In our previous study, we found that APTX interacts with X-ray repair cross-complementing group 1 (XRCC1), a scaffold protein with an essential role in single-strand DNA break repair (SSBR). To further characterize the functions of APTX, we determined the domains of APTX and XRCC1 required for the interaction. We demonstrated that the 20 N-terminal amino acids of the FHA domain of APTX are important for its interaction with the C-terminal region (residues 492-574) of XRCC1. Moreover, we found that poly (ADP-ribose) polymerase-1 (PARP-1) is also co-immunoprecipitated with APTX. These findings suggest that APTX, together with XRCC1 and PARP-1, plays an essential role in SSBR.

Pubmed ID: 15555565 RIS Download

Mesh terms: Amino Acid Sequence | Binding Sites | Cell Line | DNA-Binding Proteins | Humans | Kidney | Molecular Sequence Data | Nuclear Proteins | Protein Binding | Protein Structure, Tertiary | Recombinant Proteins | Sequence Analysis, Protein | Sequence Homology, Amino Acid | Structure-Activity Relationship | Two-Hybrid System Techniques

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