Related domains in yeast tRNA ligase, bacteriophage T4 polynucleotide kinase and RNA ligase, and mammalian myelin 2',3/‐cyclic nucleotide phosphohydrolase revealed by amino acid squence comparison
Related domains in yeast tRNA ligase, bacteriophage T4 polynucleotide kinase and RNA ligase, and mammalian myelin 2',3/‐cyclic nucleotide phosphohydrolase revealed by amino acid squence comparison
复制标题
通过氨基酸序列比较揭示酵母 tRNA 连接酶、噬菌体 T4 多核苷酸激酶和 RNA 连接酶以及哺乳动物髓磷脂 2,3/-环核苷酸磷酸水解酶中的相关结构域
DOI:
10.1016/0014-5793(90)81015-g
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发表时间:
1990
期刊:
影响因子:
3.5
通讯作者:
A. Gorbalenya
中科院分区:
文献类型:
--
作者:
E. Koonin;A. Gorbalenya
Related domains containing the purine NTP-binding sequence pattern have been revealed in two enzymes involved in tRNA processing, yeast tRNA ligase and phage T4 polynucleotide kinase, and in one of the major proteins of mammalian nerve myelin sheath, 2',3'-cyclic nucleotide 3'-phospho-hydrolase (CNPase). It is suggested that, similarly to the tRNA processing enzymes, CNPase possesses polynucleotide kinase activity, in addition to the phosphohydrolase one. It is speculated that CNPase may be an authentic mammalian polynucleotide kinase recruited as a structural component of the myelin sheath, analogously to the eye lens crystallins. Significant sequence similarity was revealed also between the N-terminal regions of yeast tRNA ligase and phage T4 RNA ligase. A tentative scheme of the domainal organizations for the three complex enzymes is proposed. According to this model, tRNA ligase contains at least three functional domains, in the order: N-ligase-kinase-phosphohydrolase-C, whereas poly-nucleotide kinase and CNPase encompass only the two C-terminal domains in the same order.
DOI:
--
发表时间:
1988
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Westaway,SK;Phizicky,EM;Abelson,J
通讯作者:
Abelson,J
DOI:
--
发表时间:
1987
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Kurihara,T;Fowler,AV;Takahashi,Y
通讯作者:
Takahashi,Y