Intrinsic apurinic/apyrimidinic (AP) endonuclease activity enables Bacillus subtilis DNA polymerase X to recognize, incise, and further repair abasic sites

The N-glycosidic bond can be hydrolyzed spontaneously or by glycosylases during removal of damaged bases by the base excision repair pathway, leading to the formation of highly mutagenic apurinic/apyrimidinic (AP) sites. Organisms encode for evolutionarily conserved repair machinery, including speci...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2010-11, Vol.107 (45), p.19219-19224
Main Authors: Baños, Benito, Villar, Laurentino, Salas, Margarita, de Vega, Miguel
Format: Article
Language:English
Subjects:
Active sites
Bacillus subtilis
Bacillus subtilis - enzymology
Bacteria
Biological Sciences
Catalysis
Deoxyribonucleic acid
DNA
DNA damage
DNA polymerase
DNA Repair
DNA-(Apurinic or Apyrimidinic Site) Lyase - metabolism
DNA-Directed DNA Polymerase - genetics
Enzymes
Mutagenesis
Nucleic acids
Nucleotides
Oligonucleotides
Polymerization
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Summary:The N-glycosidic bond can be hydrolyzed spontaneously or by glycosylases during removal of damaged bases by the base excision repair pathway, leading to the formation of highly mutagenic apurinic/apyrimidinic (AP) sites. Organisms encode for evolutionarily conserved repair machinery, including specific AP endonucleases that cleave the DNA backbone 5' to the AP site to prime further DNA repair synthesis. We report on the DNA polymerase X from the bacterium Bacillus subtilis (PolX Bs ) that, along with polymerization and 3'–5'-exonuclease activities, possesses an intrinsic AP-endonuclease activity. Both, AP-endonuclease and 3'–5'-exonuclease activities are genetically linked and governed by the same metal ligands located at the C-terminal polymerase and histidinol phosphatase domain of the polymerase. The different catalytic functions of PolX Bs enable it to perform recognition and incision at an AP site and further restoration (repair) of the original nucleotide in a standalone AP-endonuclease-independent way.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1013603107