Structural basis for aminoacylation of cellular modified tRNA^Lys3 by human lysyl-tRNA synthetase.

ABSTRACT: The average eukaryotic tRNA contains 13 posttranscriptional modifications; however, their functional impact is largely unknown. Our understanding of the complex tRNA aminoacylation machinery in metazoans also remains limited. Herein, using a series of high-resolution cryo-electron microscopy (cryo-EM) structures, we provide the mechanistic basis for recognition and aminoacylation of fully-modified cellular tRNA^Lys3 by human lysyl-tRNA synthetase (h-LysRS). The tRNA^Lys3 anticodon loop modifications S34 (mcm⁵s²U) and R37 (ms²t⁶A) play an integral role in recognition by h-LysRS. Modifications in the T-, variable-, and D-loops of tRNA^Lys3 are critical for ordering the metazoan-specific N-terminal domain of LysRS. The

SUBMITTER: Devarkar SC 

PROVIDER: S-EPMC11643047 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature