The nucleoside triphosphate-ribonucleic acid nucleotidyltransferase (EC 2.7.7.6) of Agrobacterium tumefaciens (Smith and Townsend) Conn. Purification and properties of the enzyme from the tumorigenic strain B6806.
The nucleoside triphosphate-ribonucleic acid nucleotidyltransferase (EC 2.7.7.6) of Agrobacterium tumefaciens (Smith and Townsend) Conn. Purification and properties of the enzyme from the tumorigenic strain B6806.
复制标题
根癌农杆菌(Smith 和 Townsend)康涅狄格州的核苷三磷酸核糖核酸核苷酸转移酶 (EC 2.7.7.6)。来自致瘤菌株 B6806 的酶的纯化和特性。
DOI:
10.1042/bj1430511
复制
发表时间:
1974
影响因子:
4.1
通讯作者:
U. C. Knopf
中科院分区:
文献类型:
--
作者:
U. C. Knopf
The RNA nucleotidyltransferase (RNA polymerase) of the plant-tumorigenic bacterium Agrobacterium tumefaciens was purified. The method involves the disruption of the bacterial cells with glass beads in a Waring Blendor, treatment with DEAE-cellulose, fractionation with (NH(4))(2)SO(4), protamine sulphate precipitation, DEAE-cellulose column chromatography and either glycerol-gradient centrifugation or phosphocellulose chromatography. The subunit structure of the highly purified enzyme is similar to, although not identical with, the RNA nucleotidyltransferase of Escherichia coli. It can be described as beta', beta, chi(1) and alpha (mol.wts. 160000, 150000, 98000, and 41000+/-10% respectively). chi(1) is the temporary designation for a protein subunit, which might have the same functions as the sigma subunit in E. coli. The enzyme of A. tumefaciens is rifampicin-sensitive, has a temperature optimum in vitro of 41+/-1 degrees C and a pH optimum of 8.2+/-0.1. Mg(2+) and Mn(2+) are activators. The enzyme transcribes with different efficiencies artificial, viral, bacterial, plant and animal templates.