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(Received for publication, July 7, 1997)
From the Centro de Biología Molecular "Severo Ochoa"
(C.S.I.C.-U.A.M.), Universidad Autónoma, Canto Blanco,
28049 Madrid, Spain
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
Volume 272, Number 49,
Issue of December 5, 1997
pp. 30899-30910
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Characterization of an African Swine Fever Virus 20-kDa DNA
Polymerase Involved in DNA Repair
-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 
(pol ), 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 -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.
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