DNA-binding activity of amino-terminal domains of the Bacillus subtilis AbrB protein.
DNA-binding activity of amino-terminal domains of the Bacillus subtilis AbrB protein.
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枯草芽孢杆菌 AbrB 蛋白氨基末端结构域的 DNA 结合活性。
DOI：
10.1128/jb.183.13.4094-4098.2001
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发表时间：
2001
影响因子：
3.2
通讯作者：
Strauch,MA
中科院分区：
文献类型：
--
作者：
Xu,K;Strauch,MA
构建并纯化了AbrB的两个截断变体，分别包含其前53个（AbrBN53）或前55个（AbrBN55）氨基酸残基。截断变异的非共价连锁同二聚体表现出非常弱的dna结合活性。将AbrBN55二聚体交联成四聚体和高阶多聚体（通过第二半胱氨酸残基之间的二硫键结合），导致蛋白质具有与完整的野生型AbrB相当的dna结合亲和力和相同的dna结合特异性。这些结果表明，AbrB结合的DNA识别和特异性决定因素仅存在于其n端氨基酸序列中。
Two truncated variants of AbrB, comprising either its first 53 (AbrBN53) or first 55 (AbrBN55) amino acid residues, were constructed and purified. Noncovalently linked homodimers of the truncated variants exhibited very weak DNA-binding activity. Cross-linking AbrBN55 dimers into tetramers and higher-order multimers (via disulfide bonding between penultimate cysteine residues) resulted in proteins having DNA-binding affinity comparable to and DNA-binding specificity identical to those of intact, wild-type AbrB. These results indicate that the DNA recognition and specificity determinants of AbrB binding lie solely within its N-terminal amino acid sequence.