The oligomerization of CynR in Escherichia coli
The oligomerization of CynR in Escherichia coli
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DOI：
10.1002/pro.241
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发表时间：
2009-11-01
期刊：
影响因子：
8
通讯作者：
Hu, James C.
中科院分区：
文献类型：
--
作者：
Knapp, Gwendowlyn S.;Hu, James C.
缺失分析和丙氨酸扫描的基础上的同源性为基础的相互作用模型被用来确定寡聚化的转录调节CynR，LysR型转录调节因子（LTTR）家族的成员的决定因素。缺失分析证实，CynR的推定调节结构域对于驱动λ阻遏物-CynR融合蛋白的寡聚化至关重要。将不同LTTR和OxyR的相互作用表面映射到LTTR家族的多序列比对上。该映射确定了CynR调节结构域二聚体界面中的推定接触，其被靶向丙氨酸扫描诱变。寡聚化通过突变λ阻遏物-CynR融合体在E.揭示了OxyR和CynR之间有趣的相似性和差异。
Deletion analysis and alanine-scanning based on a homology-based interaction model were used to identify determinants of oligomerization in the transcriptional regulator CynR, a member of the LysR-type transcriptional regulator (LTTR) family. Deletion analysis confirmed that the putative regulatory domain of CynR was essential for driving the oligomerization of lambda repressor-CynR fusion proteins. The interaction surface of a different LTTR and OxyR was mapped onto a multiple sequence alignment of the LTTR family. This mapping identified putative contacts in the CynR regulatory domain dimer interface, which were targeted for alanine-scanning mutagenesis. Oligomerization was assayed by the ability of mutant lambda repressor-CynR fusions to assemble in E. coli revealing interesting similarities and differences between OxyR and CynR.