Structural and functional relationships between prokaryotic and eukaryotic DNA polymerases.
作者： A. Bernad , A. Zaballos , M. Salas , L. Blanco
DOI: 10.1002/J.1460-2075.1987.TB02770.X
关键词:
摘要: The Bacillus subtilis phage luminal diameter 29 DNA polymerase, involved in protein-primed viral replication, was inhibited by phosphonoacetic acid (PAA), a known inhibitor of alpha-like polymerases, decreasing the rate elongation. Three highly conserved regions amino homology, found several polymerases and one them proposed to be PAA binding site, were also T4 polymerase. This prokaryotic enzyme sensitive drugs aphidicolin nucleotide analogues butylanilino dATP (BuAdATP) butylphenyl dGTP (BuPdGTP), specific inhibitors eukaryotic polymerases. Two potential from linear plasmid pGKL1 yeast S1 mitochondrial maize have been identified, based on fact that they contain three homology. Comparison origin showed extensive homology addition domains. These findings reflect evolutionary relationships between hypothetically unrelated
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