On the Mechanism and Origin of Isoleucyl-tRNA Synthetase Editing against Norvaline.
aminoacyl-tRNA synthetase
mistranslation
non-proteinogenic amino acids
primordial translation
proofreading
Journal
Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R
Informations de publication
Date de publication:
15 03 2019
15 03 2019
Historique:
received:
16
12
2018
revised:
20
01
2019
accepted:
22
01
2019
pubmed:
4
2
2019
medline:
24
3
2020
entrez:
4
2
2019
Statut:
ppublish
Résumé
Aminoacyl-tRNA synthetases (aaRSs), the enzymes responsible for coupling tRNAs to their cognate amino acids, minimize translational errors by intrinsic hydrolytic editing. Here, we compared norvaline (Nva), a linear amino acid not coded for protein synthesis, to the proteinogenic, branched valine (Val) in their propensity to mistranslate isoleucine (Ile) in proteins. We show that in the synthetic site of isoleucyl-tRNA synthetase (IleRS), Nva and Val are activated and transferred to tRNA at similar rates. The efficiency of the synthetic site in pre-transfer editing of Nva and Val also appears to be similar. Post-transfer editing was, however, more rapid with Nva and consequently IleRS misaminoacylates Nva-tRNA
Identifiants
pubmed: 30711543
pii: S0022-2836(19)30046-4
doi: 10.1016/j.jmb.2019.01.029
pii:
doi:
Substances chimiques
Escherichia coli Proteins
0
norvaline
A70UKS48FE
Isoleucine-tRNA Ligase
EC 6.1.1.5
Valine
HG18B9YRS7
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1284-1297Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.