ANGEL2 phosphatase activity is required for non-canonical mitochondrial RNA processing.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
30 09 2022
30 09 2022
Historique:
received:
15
03
2022
accepted:
14
09
2022
entrez:
30
9
2022
pubmed:
1
10
2022
medline:
5
10
2022
Statut:
epublish
Résumé
Canonical RNA processing in mammalian mitochondria is defined by tRNAs acting as recognition sites for nucleases to release flanking transcripts. The relevant factors, their structures, and mechanism are well described, but not all mitochondrial transcripts are punctuated by tRNAs, and their mode of processing has remained unsolved. Using Drosophila and mouse models, we demonstrate that non-canonical processing results in the formation of 3' phosphates, and that phosphatase activity by the carbon catabolite repressor 4 domain-containing family member ANGEL2 is required for their hydrolysis. Furthermore, our data suggest that members of the FAST kinase domain-containing protein family are responsible for these 3' phosphates. Our results therefore propose a mechanism for non-canonical RNA processing in metazoan mitochondria, by identifying the role of ANGEL2.
Identifiants
pubmed: 36180430
doi: 10.1038/s41467-022-33368-9
pii: 10.1038/s41467-022-33368-9
pmc: PMC9525292
doi:
Substances chimiques
Phosphates
0
RNA, Mitochondrial
0
RNA
63231-63-0
Carbon
7440-44-0
RNA, Transfer
9014-25-9
Exoribonucleases
EC 3.1.-
Phosphoric Monoester Hydrolases
EC 3.1.3.2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
5750Informations de copyright
© 2022. The Author(s).
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