The role of tRNA identity elements in aminoacyl-tRNA editing.

aminoacyl-tRNA synthetases editing mistranslation protein synthesis tRNA translational fidelity

Journal

Frontiers in microbiology
ISSN: 1664-302X
Titre abrégé: Front Microbiol
Pays: Switzerland
ID NLM: 101548977

Informations de publication

Date de publication:
2024
Historique:
received: 23 05 2024
accepted: 18 06 2024
medline: 5 8 2024
pubmed: 5 8 2024
entrez: 5 8 2024
Statut: epublish

Résumé

The rules of the genetic code are implemented by the unique features that define the amino acid identity of each transfer RNA (tRNA). These features, known as "identity elements," mark tRNAs for recognition by aminoacyl-tRNA synthetases (ARSs), the enzymes responsible for ligating amino acids to tRNAs. While tRNA identity elements enable stringent substrate selectivity of ARSs, these enzymes are prone to errors during amino acid selection, leading to the synthesis of incorrect aminoacyl-tRNAs that jeopardize the fidelity of protein synthesis. Many error-prone ARSs have evolved specialized domains that hydrolyze incorrectly synthesized aminoacyl-tRNAs. These domains, known as editing domains, also exist as free-standing enzymes and, together with ARSs, safeguard protein synthesis fidelity. Here, we discuss how the same identity elements that define tRNA aminoacylation play an integral role in aminoacyl-tRNA editing, synergistically ensuring the correct translation of genetic information into proteins. Moreover, we review the distinct strategies of tRNA selection used by editing enzymes and ARSs to avoid undesired hydrolysis of correctly aminoacylated tRNAs.

Identifiants

pubmed: 39101037
doi: 10.3389/fmicb.2024.1437528
pmc: PMC11295145
doi:

Types de publication

Journal Article Review

Langues

eng

Pagination

1437528

Informations de copyright

Copyright © 2024 Cruz and Vargas-Rodriguez.

Déclaration de conflit d'intérêts

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Auteurs

Edwin Cruz (E)

Department of Molecular Biology and Biophysics, University of Connecticut School of Medicine, Farmington, CT, United States.

Oscar Vargas-Rodriguez (O)

Department of Molecular Biology and Biophysics, University of Connecticut School of Medicine, Farmington, CT, United States.

Classifications MeSH