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

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


  • Date H
  • Igarashi S
  • Sano Y
  • Takahashi T
  • Takahashi T
  • Takano H
  • Tsuji S
  • Nishizawa M
  • Onodera O


Biochemical and biophysical research communications

Publication Data

December 24, 2004

Associated Grants


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