STRUCTURAL AND FUNCTIONAL-RELATIONSHIPS BETWEEN PROKARYOTIC AND EUKARYOTIC DNA-POLYMERASES
STRUCTURAL AND FUNCTIONAL-RELATIONSHIPS BETWEEN PROKARYOTIC AND EUKARYOTIC DNA-POLYMERASES
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DOI:
10.1002/j.1460-2075.1987.tb02770.x
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发表时间:
1987-12-01
期刊:
影响因子:
11.4
通讯作者:
BLANCO, L
中科院分区:
文献类型:
--
作者:
BERNAD, A;ZABALLOS, A;BLANCO, L
The Bacillus subtilis phage .vphi.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 .vphi.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. Comarison 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.