Ohnishi K
Department of Biology, Faculty of Science, Niigata University, Japan.
Nucleic Acids Symp Ser. 1988(19):193-7.
Alignment of the amino acid (aa) sequences of T7 phage DNA polymerase (DPase), E. coli DNA polymerase I (Pol I) and MS2 phage RNA replicase beta subunit (MS2 Repl) were established by computer-aided methods. The results showed that the entire length (aa's 16-704) of T7 DPase is homologous to Pol I aa's 207-928(C-term) with 21.5% aa identity, and that domains I (aa's-1-311) and II (312-451(C-term] were found to be homologous to each other and to N-terminal region of T7 DPase (aa's 1-250). Thus these enzymes and domains are homologous to one another and must have evolved from a co-ancestral enzyme.
通过计算机辅助方法对T7噬菌体DNA聚合酶(DPase)、大肠杆菌DNA聚合酶I(Pol I)和MS2噬菌体RNA复制酶β亚基(MS2 Repl)的氨基酸(aa)序列进行了比对。结果表明,T7 DPase的全长(氨基酸16 - 704)与Pol I的氨基酸207 - 928(C端)同源,氨基酸同一性为21.5%,并且发现结构域I(氨基酸 - 1 - 311)和结构域II(312 - 451(C端))彼此同源,且与T7 DPase的N端区域(氨基酸1 - 250)同源。因此,这些酶和结构域彼此同源,必定是从共同的祖先酶进化而来的。