Article
Structure-function analysis of Sua5 protein reveals novel functional motifs required for the biosynthesis of the universal t6A tRNA modification.
RNA (New York, N.Y.) - 1 Jul 2018
Pichard-Kostuch Adeline, Zhang Wenhua, Liger Dominique, Daugeron Marie-Claire, Létoquart Juliette, Li de la Sierra-Gallay Ines, Forterre Patrick, Collinet Bruno, van Tilbeurgh Herman, Basta Tamara
Abstract excerpt
N6-threonyl-carbamoyl adenosine (t6A) is a universal tRNA modification found at position 37, next to the anticodon, in almost all tRNAs decoding ANN codons (where N = A, U, G, or C). t6A stabilizes the codon-anticodon interaction and hence promotes translation fidelity. The first step of the biosynthesis of t6A, the production of threonyl-carbamoyl adenylate (TC-AMP), is catalyzed by the Sua5/TsaC family of...
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