Chiral proofreading during protein biosynthesis and its evolutionary implications.
Homochirality
aminoacyl-tRNA synthetase
chiral proofreading
d-amino acids
endosymbiosis
mitochondria
protein biosynthesis
tRNA
translation of genetic code
translation quality control
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
07 2022
07 2022
Historique:
revised:
16
05
2022
received:
31
03
2022
accepted:
29
05
2022
pubmed:
7
6
2022
medline:
14
7
2022
entrez:
6
6
2022
Statut:
ppublish
Résumé
Homochirality of biomacromolecules is a prerequisite for their proper functioning and hence essential for all life forms. This underscores the role of cellular chiral checkpoints in enforcing homochirality during protein biosynthesis. d-Aminoacyl-tRNA deacylase (DTD) is an enzyme that performs 'chirality-based proofreading' to remove d-amino acids mistakenly attached to tRNAs, thus recycling them for further rounds of translation. Paradoxically, owing to its l-chiral rejection mode of action, DTD can remove glycine as well, which is an achiral amino acid. However, this activity is modulated by discriminator base (N73) in tRNA, a unique element that protects the cognate Gly-tRNA
Identifiants
pubmed: 35662005
doi: 10.1002/1873-3468.14419
doi:
Substances chimiques
Amino Acids
0
RNA, Transfer, Amino Acyl
0
RNA, Transfer, Gly
0
RNA, Transfer
9014-25-9
Glycine
TE7660XO1C
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1615-1627Informations de copyright
© 2022 Federation of European Biochemical Societies.
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