Structural basis for impaired 5' processing of a mutant tRNA associated with defects in neuronal homeostasis.

Lai, Lien B; Lai, Stella M; Szymanski, Eric S; Kapur, Mridu; Choi, Edric K; Al-Hashimi, Hashim M; Ackerman, Susan L; Gopalan, Venkat · Proc Natl Acad Sci U S A · 2022

basic_science · Level V

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Abstract

SignificanceUnderstanding and treating neurological disorders are global priorities. Some of these diseases are engendered by mutations that cause defects in the cellular synthesis of transfer RNAs (tRNAs), which function as adapter molecules that translate messenger RNAs into proteins. During tRNA biogenesis, ribonuclease P catalyzes removal of the transcribed sequence upstream of the mature tRNA. Here, we focus on a cytoplasmic tRNA<sup>Arg</sup><sub>UCU</sub> that is expressed specifically in neurons and, when harboring a particular point mutation, contributes to neurodegeneration in mice. Our results suggest that this mutation favors stable alternative structures that are not cleaved by mouse ribonuclease P and motivate a paradigm that may help to understand the molecular basis for disease-associated mutations in other tRNAs.

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