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

Department of Neurology, Brain Research Institute Niigata University, Nigata, Japan.
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.
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
Biochem. Biophys. Res. Commun. Dec. 24, 2004; 325(4);1279-85 [PUBMED:15555565]
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