The Bacillus stearothermophilus replicative helicase:: cloning, overexpression and activity

The Bacillus stearothermophilus replicative helicase:: cloning, overexpression and activity
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DOI:
10.1016/s0167-4781(99)00024-x
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发表时间:
1999-03-19
期刊:
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION
影响因子:
--
通讯作者:
Wigley, DB
Wigley, DB
中科院分区:
其他
文献类型:
--
作者:
Bird, LE;Wigley, DB

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作为革兰氏阳性细菌原体的生化和结构研究的一部分,我们描述了嗜热脂肪芽孢杆菌复制解旋酶DnaB的克隆。该蛋白与大肠杆菌和枯草芽孢杆菌的复制解旋酶分别有45%和82%的相同。重组DnaB被纯化并证明是一种活性解旋酶。(C) 1999 Elsevier Science B.V.版权所有
As part of biochemical and structural studies of the primosome of a Gram positive bacterial species, we describe the cloning of the Bacillus stearothermophilus replicative helicase, DnaB. The protein is 45% and 82% identical to the Escherichia coli and B. subtilis replicative helicases, respectively. Recombinant DnaB was purified and shown to be an active helicase. (C) 1999 Elsevier Science B.V. All rights reserved.