The development of novel strategies allowed Camakaris et al. (e00252-21) to isolate mutants of RpoA (α-subunit of RNA polymerase) that were defective in activation of genes of the TyrR regulon and to subsequently isolate suppressors in TyrR that partially restored activation. These data demonstrated that activation involves protein-protein interaction and helped to identify both the “TyrR-specific determinant” on RpoA and the complementary “activation patch” on the TyrR N-terminal domain, both of which are surface exposed. These studies suggest a model for activation by TyrR that involves three sites on the α subunit of the C-terminal domain, the “TyrR-specific determinant,” the “265 determinant,” and the “261 determinant.”

中文翻译：

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本期重要文章

新策略的发展使 Camakaris 等人得以发展。（e00252-21）分离 RpoA（RNA 聚合酶的α-亚基）突变体，这些突变体在 TyrR 调节子基因的激活方面存在缺陷，随后在 TyrR 中分离出部分恢复激活的抑制因子。这些数据表明，激活涉及蛋白质-蛋白质相互作用，有助于识别 RpoA 上的“TyrR 特异性决定簇”和 TyrR N 端结构域上的互补“激活补丁”，两者都是表面暴露的。这些研究提出了一个 TyrR 激活模型，该模型涉及 C 末端结构域 α 亚基上的三个位点，即“TyrR 特异性决定簇”、“265 决定簇”和“261 决定簇”。