Abstract
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.”
Accepted Version
Published Version
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