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大肠杆菌TyrR的N316突变体的寡聚化特性改变

Altered oligomerization properties of N316 mutants of Escherichia coli TyrR.

作者信息

Koyanagi Takashi, Katayama Takane, Suzuki Hideyuki, Kumagai Hidehiko

机构信息

Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.

出版信息

J Bacteriol. 2008 Dec;190(24):8238-43. doi: 10.1128/JB.00889-08. Epub 2008 Oct 17.

DOI:10.1128/JB.00889-08
PMID:18931124
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2593242/
Abstract

The transcriptional regulator TyrR is known to undergo a dimer-to-hexamer conformational change in response to aromatic amino acids, through which it controls gene expression. In this study, we identified N316D as the second-site suppressor of Escherichia coli TyrR(E274Q), a mutant protein deficient in hexamer formation. N316 variants exhibited altered in vivo regulatory properties, and the most drastic changes were observed for TyrR(N316D) and TyrR(N316R) mutants. Gel filtration analyses revealed that the ligand-mediated oligomer formation was enhanced and diminished for TyrR(N316D) and TyrR(N316R), respectively, compared with the wild-type TyrR. ADP was substituted for ATP in the oligomer formation of TyrR(N316D).

摘要

已知转录调节因子TyrR会响应芳香族氨基酸而发生从二聚体到六聚体的构象变化，通过这种变化它控制基因表达。在本研究中，我们鉴定出N316D是大肠杆菌TyrR（E274Q）的第二位点抑制子，TyrR（E274Q）是一种缺乏六聚体形成能力的突变蛋白。N316变体表现出改变的体内调节特性，其中TyrR（N316D）和TyrR（N316R）突变体的变化最为显著。凝胶过滤分析表明，与野生型TyrR相比，TyrR（N316D）的配体介导的寡聚体形成增强，而TyrR（N316R）的则减少。在TyrR（N316D）的寡聚体形成中，ADP替代了ATP。

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Crystal structure of the N-terminal domain of the TyrR transcription factor responsible for gene regulation of aromatic amino acid biosynthesis and transport in Escherichia coli K12.负责大肠杆菌K12中芳香族氨基酸生物合成与转运基因调控的TyrR转录因子N端结构域的晶体结构
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