Regulation of poly(a)-specific ribonuclease activity by reversible lysine acetylation.
RNA processing
acetylation
genome maintenance
human telomerase RNA component (hTR)
noncoding RNA
p300
poly(A)-specific ribonuclease (PARN)
polyadenylation
post-translational modification (PTM)
protein acetylation
sirtuin 1 (SIRT1)
sirtuin1 (SIRT1)
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
24 07 2020
24 07 2020
Historique:
received:
06
01
2020
revised:
20
05
2020
pubmed:
28
5
2020
medline:
14
1
2021
entrez:
28
5
2020
Statut:
ppublish
Résumé
Poly(A)-specific ribonuclease (PARN) is a 3'-exoribonuclease that plays an important role in regulating the stability and maturation of RNAs. Recently, PARN has been found to regulate the maturation of the human telomerase RNA component (hTR), a noncoding RNA required for telomere elongation. Specifically, PARN cleaves the 3'-end of immature, polyadenylated hTR to form the mature, nonpolyadenylated template. Despite PARN's critical role in mediating telomere maintenance, little is known about how PARN's function is regulated by post-translational modifications. In this study, using shRNA- and CRISPR/Cas9-mediated gene silencing and knockout approaches, along with 3'-exoribonuclease activity assays and additional biochemical methods, we examined whether PARN is post-translationally modified by acetylation and what effect acetylation has on PARN's activity. We found PARN is primarily acetylated by the acetyltransferase p300 at Lys-566 and deacetylated by sirtuin1 (SIRT1). We also revealed how acetylation of PARN can decrease its enzymatic activity both
Identifiants
pubmed: 32457045
pii: S0021-9258(17)50136-2
doi: 10.1074/jbc.RA120.012552
pmc: PMC7383379
doi:
Substances chimiques
Telomerase
EC 2.7.7.49
Exoribonucleases
EC 3.1.-
poly(A)-specific ribonuclease
EC 3.1.13.4
SIRT1 protein, human
EC 3.5.1.-
Sirtuin 1
EC 3.5.1.-
Lysine
K3Z4F929H6
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
10255-10270Subventions
Organisme : NCI NIH HHS
ID : R01 CA169210
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA187040
Pays : United States
Informations de copyright
© 2020 Dejene et al.
Déclaration de conflit d'intérêts
Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article.
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