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首页> 外文期刊>Journal of bacteriology >An N-terminal mutation in the bacteriophage T4 motA gene yields a protein that binds DNA but is defective for activation of transcription.
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An N-terminal mutation in the bacteriophage T4 motA gene yields a protein that binds DNA but is defective for activation of transcription.

机译：噬菌体T4 motA基因的N端突变产生的蛋白与DNA结合，但对转录激活有缺陷。

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摘要

The bacteriophage T4 MotA protein is a transcriptional activator of T4-modified host RNA polymerase and is required for activation of the middle class of T4 promoters. MotA alone binds to the -30 region of T4 middle promoters, a region that contains the MotA box consensus sequence [(t/a)(t/a)TGCTT(t/c)A]. We report the isolation and characterization of a protein designated Mot21, in which the first 8 codons of the wild-type motA sequence have been replaced with 11 different codons. In gel retardation assays, Mot21 and MotA bind DNA containing the T4 middle promoter P(uvsX) similarly, and the proteins yield similar footprints on P(uvsX). However, Mot21 is severely defective in the activation of transcription. On native protein gels, a new protein species is seen after incubation of the sigma70 subunit of RNA polymerase and wild-type MotA protein, suggesting a direct protein-protein contact between MotA and sigma70. Mot21 fails to form this complex, suggesting that this interaction is necessary for transcriptional activation and that the Mot21 defect arises because Mot21 cannot form this contact like the wild-type activator.
机译：噬菌体T4 MotA蛋白是T4修饰的宿主RNA聚合酶的转录激活因子，是激活T4中型启动子所需的。 MotA单独与T4中间启动子的-30区结合，该区域包含MotA框共有序列[（t / a）（t / a）TGCTT（t / c）A]。我们报告了分离和表征的蛋白质称为Mot21，其中野生型motA序列的前8个密码子已被11个不同的密码子代替。在凝胶阻滞测定中，Mot21和MotA相似地结合包含T4中间启动子P（uvsX）的DNA，并且蛋白质在P（uvsX）上产生相似的足迹。但是，Mot21在转录激活方面存在严重缺陷。在天然蛋白凝胶上，RNA聚合酶的sigma70亚基和野生型MotA蛋白经过孵育后，会发现一种新的蛋白，这表明MotA与sigma70之间存在直接的蛋白-蛋白接触。 Mot21无法形成这种复合物，表明该相互作用对于转录激活是必需的，并且由于Mot21无法像野生型激活剂一样形成这种接触，因此出现Mot21缺陷。

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