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Structural and functional relationships between prokaryotic and eukaryotic DNA polymerases.
Author(s) -
Bernad A.,
Zaballos A.,
Salas M.,
Blanco L.
Publication year - 1987
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1987.tb02770.x
Subject(s) - biology , dna polymerase , genetics , polymerase , dna , computational biology , primase , evolutionary biology , polymerase chain reaction , gene , reverse transcriptase
The Bacillus subtilis phage luminal diameter 29 DNA polymerase, involved in protein‐primed viral DNA replication, was inhibited by phosphonoacetic acid (PAA), a known inhibitor of alpha‐like DNA polymerases, by decreasing the rate of elongation. Three highly conserved regions of amino acid homology, found in several viral alpha‐like DNA polymerases and in the luminal diameter 29 DNA polymerase, one of them proposed to be the PAA binding site, were also found in the T4 DNA polymerase. This prokaryotic enzyme was highly sensitive to the drugs aphidicolin and the nucleotide analogues butylanilino dATP (BuAdATP) and butylphenyl dGTP (BuPdGTP), known to be specific inhibitors of eukaryotic alpha‐like DNA polymerases. Two potential DNA polymerases from the linear plasmid pGKL1 from yeast and the S1 mitochondrial DNA from maize have been identified, based on the fact that they contain the three conserved regions of amino acid homology. Comparison of DNA polymerases from prokaryotic and eukaryotic origin showed extensive amino acid homology in addition to highly conserved domains. These findings reflect evolutionary relationships between hypothetically unrelated DNA polymerases.