大肠杆菌的Hha蛋白对H-NS寡聚结构域的功能替代。
Functional replacement of the oligomerization domain of H-NS by the Hha protein of Escherichia coli.
作者信息
Rodríguez Sonia, Nieto José María, Madrid Cristina, Juárez Antonio
机构信息
Departament de Microbiologia, Facultat de Biologia, Universitat de Barcelona, Avda. Diagonal 645, 08028 Barcelona, Spain.
出版信息
J Bacteriol. 2005 Aug;187(15):5452-9. doi: 10.1128/JB.187.15.5452-5459.2005.
Abstract
Members of the H-NS family of proteins play a relevant role as modulators of gene expression in gram-negative bacteria. Interaction of these proteins with members of the Hha/YmoA family of proteins has been previously reported. It has been hypothesized that the latter proteins are functionally equivalent to the N-terminal domain of H-NS-like proteins. In this report we test this assumption by replacing the N-terminal domain of Escherichia coli H-NS by Hha. It has been possible to obtain a functional protein that can compensate for some of the hns-induced phenotypes. These results highlight the relevance of H-NS-Hha interactions to generate heterooligomeric complexes that modulate gene expression in gram-negative bacteria.
摘要
H-NS蛋白家族成员作为革兰氏阴性菌中基因表达的调节因子发挥着重要作用。此前已有报道称这些蛋白与Hha/YmoA蛋白家族成员存在相互作用。据推测，后一类蛋白在功能上等同于H-NS样蛋白的N端结构域。在本报告中，我们通过用Hha替换大肠杆菌H-NS的N端结构域来验证这一假设。我们成功获得了一种功能性蛋白，它可以弥补一些hns诱导的表型。这些结果突出了H-NS与Hha相互作用对于生成调节革兰氏阴性菌基因表达的异源寡聚复合物的重要性。
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