Abstract:The universal N(6)‐threonylcarbamoyladenosine (t6A) modification at position 37 of ANN‐decoding tRNAs is central to translational fidelity. In bacteria, t6A biosynthesis is catalyzed by the proteins TsaB, TsaC/TsaC2, TsaD, and TsaE. Despite intense research, the molecular mechanisms underlying t6A biosynthesis are poorly understood. Here we report biochemical and biophysical studies of the t6A biosythesis system from Thermotoga maritima. Small angle X‐ray scattering analysis reveals a symmetric 2:2 stoichiomet… Show more
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