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AP‐site cleavage activity of tyrosyl‐DNA phosphodiesterase 1
Author(s) -
Lebedeva Natalia A.,
Rechkunova Nadejda I.,
Lavrik Olga I.
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.01.032
Subject(s) - dna polymerase beta , base excision repair , dna polymerase , dna ligase , ap endonuclease , microbiology and biotechnology , dna repair , chemistry , dna , cleavage (geology) , xrcc1 , parp1 , biochemistry , biology , polymerase , poly adp ribose polymerase , gene , paleontology , fracture (geology) , genotype , single nucleotide polymorphism
APE‐independent base excision repair (BER) pathway plays an important role in the regulation of DNA repair mechanisms. In this study it has been found that recently discovered tyrosyl‐DNA phosphodiesterase 1 (Tdp1) catalyzes the AP site cleavage reaction to generate breaks with the 3′‐ and 5′‐phosphate termini. The removal of the 3′‐phosphate is performed by polynucleotide kinase phosphatase (PNKP). Tdp1 is known to interact stably with BER proteins: DNA polymerase beta (Pol β), XRCC1, PARP1 and DNA ligase III. The data suggest a role of Tdp1 in the new APE‐independent BER pathway in mammals.