| First Author | Oliveros M | Year | 1997 |
| Journal | J Biol Chem | Volume | 272 |
| Issue | 49 | Pages | 30899-910 |
| PubMed ID | 9388236 | Mgi Jnum | J:44437 |
| Mgi Id | MGI:1100213 | Doi | 10.1074/jbc.272.49.30899 |
| Citation | Oliveros M, et al. (1997) Characterization of an African swine fever virus 20-kDa DNA polymerase involved in DNA repair. J Biol Chem 272(49):30899-910 |
| abstractText | African swine fever virus (ASFV) encodes a novel DNA polymerase, constituted of only 174 amino acids, belonging to the polymerase (pol) X family of DNA polymerases. Biochemical analyses of the purified enzyme indicate that ASFV pol X is a monomeric DNA-directed DNA polymerase, highly distributive, lacking a proofreading 3'-5'-exonuclease, and with a poor discrimination against dideoxynucleotides. A multiple alignment of family X DNA polymerases, together with the extrapolation to the crystal structure of mammalian DNA polymerase beta (pol beta), showed the conservation in ASFV pol X of the most critical residues involved in DNA binding, nucleotide binding, and catalysis of the polymerization reaction. Therefore, the 20-kDa ASFV pol X most likely represents the minimal functional version of an evolutionarily conserved pol beta-type DNA polymerase core, constituted by only the palm and thumb subdomains. It is worth noting that such an unfingered DNA polymerase is able to handle templated DNA polymerization with a considerable high fidelity at the base discrimination level. Base excision repair is considered to be a cellular defense mechanism repairing modified bases in DNA. Interestingly, the fact that ASFV pol X is able to conduct filling of a single nucleotide gap points to a putative role in base excision repair during the ASFV life cycle. |
