Forward genetic approach identifies a phylogenetically conserved serine residue critical for the catalytic activity of UBIQUITIN-SPECIFIC PROTEASE 12 in Arabidopsis.
Circadian clock
De-ubiquitination
Flowering time
Phosphorylation
UBP12
Ubiquitin proteases
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
25 Oct 2024
25 Oct 2024
Historique:
received:
04
06
2024
accepted:
21
10
2024
medline:
26
10
2024
pubmed:
26
10
2024
entrez:
25
10
2024
Statut:
epublish
Résumé
Circadian clocks rely on transcriptional/translational feedback loops involving clock genes and their corresponding proteins. While the primary oscillations originate from gene expression, the precise control of clock protein stability plays a pivotal role in establishing the 24-hour circadian rhythms. Most clock proteins are degraded through the ubiquitin/26S proteasome pathway, yet the enzymes responsible for ubiquitination and deubiquitination remain poorly characterised. We identified a missense allele (ubp12-3, S327F) of the UBP12 gene/protein in Arabidopsis. Despite ubp12-3 exhibited a short period phenotype similar to that of a loss-of-function allele, molecular analysis indicated elevated protease activity in ubp12-3. We demonstrated that early flowering of ubp12 mutants is a result of the shortened circadian period rather than a direct alteration of UBP12 function. Analysis of protease activity of non-phosphorylatable (S327A, S327F) and phosphomimetic (S327D) derivatives in bacteria suggested that phosphorylation of serine 327 inhibits UBP12 enzymatic activity, which could explain the over-functioning of S327F in vivo. We showed that phosphomimetic mutations of the conserved serine in the Neurospora and human orthologues reduced ubiquitin cleavage activity suggesting that not only the primary structures of UBP12-like enzymes are phylogenetically conserved across a wide range of species, but also the molecular mechanisms governing their enzymatic activity.
Identifiants
pubmed: 39455703
doi: 10.1038/s41598-024-77232-w
pii: 10.1038/s41598-024-77232-w
doi:
Substances chimiques
Arabidopsis Proteins
0
Serine
452VLY9402
UBP12 protein, Arabidopsis
EC 3.4.99.-
Ubiquitin-Specific Proteases
EC 3.4.19.12
Endopeptidases
EC 3.4.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
25273Subventions
Organisme : National Research, Development and Innovation Office
ID : K-134567
Organisme : National Research, Development and Innovation Office
ID : K-139349
Organisme : National Research, Development and Innovation Office
ID : K-134567
Organisme : Hungarian Academy of Sciences
ID : KGYNK-2023
Informations de copyright
© 2024. The Author(s).
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