EC Number   |
General Information |
Reference  |
|---|
   3.6.1.71 | physiological function |
poly-ADP ribose polymerase PARP-1 is required in the recruitment of aprataxin to sites of DNA breaks. Inhibition of PARP activity does not affect aprataxin activity in vitro, it retards its recruitment to sites of DNA damage in vivo |
703960 |
| 3.6.1.71 | physiological function |
the long-form but not the short-form aprataxin interacts with x-ray repair cross-complementing group XRCC1. Aprataxin and XRCC1 may constitute a multiprotein complex and are involved in single-strand DNA break repair |
739862 |
| 3.6.1.71 | physiological function |
APTX interacts with X-ray repair cross-complementing group XRCC1, which has an essential role in single-strand DNA break repair. The 20 N-terminal amino acids of the forkhead-associated FHA-domain of APTX are important for its interaction with the C-terminal region (residues 492574) of XRCC1. Poly(ADPribose) polymerase PARP-1 is also co-immunoprecipitated with APTX |
739976 |
| 3.6.1.71 | physiological function |
aprataxin is directly involved in DNA single-strand-break repair |
740277 |
| 3.6.1.71 | physiological function |
deletion of the Saccharomyces cerevisiae Hnt3 gene, which encodes the aprataxin homolog, in combination with known DNA repair genes. While Hnt3 single mutants are not sensitive to DNA damaging agents, loss of Hnt3 causes synergistic sensitivity to H2O2 in backgrounds that accumulate strand breaks with blocked termini, including lack of Apn1, Apn2, Tpp1 and Ntg1, Ntg2, Ogg1. Loss of HNT3 in Rad27 mutant cells, which are deficient in long-patch base excision repair, results in synergistic sensitivity to H2O2 and methylmethane sulfonate. Loss of Hnt3 also increases the sister chromatid exchange frequency. Hnt3 deletion partially rescues H2O2 sensitivity in recombination-deficient mutant Rad51 and mutant Rad52 cells |
740352 |
| 3.6.1.71 | physiological function |
aprataxin interacts with the repair proteins XRCC1, PARP-1 and p53 and colocalizes with XRCC1 along charged particle tracks on chromatin |
740518 |
| 3.6.1.71 | physiological function |
interaction between aprataxin and nucleolin occurs through their respective N-terminal regions. In cells from patients with ataxia with oculomotor apraxia type 1, AOA1, lacking aprataxin, the stability of nucleolin is significantly reduced. Down-regulation of nucleolin by RNA interference does not affect aprataxin protein levels but abolishes its nucleolar localization |
740519 |
| 3.6.1.71 | physiological function |
aprataxin has dual DNA binding and nucleotide hydrolase activities. The protein binds to double-stranded DNA with high affinity but is also capable of binding double-stranded RNA and single-strand DNA, with increased affinity for hairpin structures. The DNA binding is not dependent on zinc |
740679 |
| 3.6.1.71 | physiological function |
the protein is composed of three domains that share distant homology with the amino-terminal domain of polynucleotide kinase 3'-phosphatase, with histidine-triad proteins and with DNA-binding C2H2 zinc-finger proteins, respectively |
741055 |
| 3.6.1.71 | physiological function |
during repair of non-canonical ribonucleotides introduced into DNA during replication of the nuclear genome, DNA ligases generate 5'-adenylated RNA-DNA junctions repaired by Aptx deadenylase. In the proposed reaction scheme, step 1 generates an enzyme-AMP intermediate, which is then resolved via hydrolysis |
741062 |
