PXD043217

PXD043217 is an original dataset announced via ProteomeXchange.

Title	Global and protein-specific analysis reveals Nt-acetylation-independent turnover of SQE1 by Arabidopsis DOA10-like E3 ligases
Description	The Acetylation-dependent (Ac/) N-degron pathway degrades proteins through recognition of their acetylated N-termini (Nt) by specific E3-ligases (Ac/N-recognins). To date, no Ac/N-recognins have been defined in plants. Here we use molecular, genetic, and multi-omics approaches to characterise potential roles for Arabidopsis DOA10-like E3-ligases in the Nt-acetylation-(NTA-) dependent turnover of proteins at global and protein-specific scales. Arabidopsis has two ER-localised DOA10-like proteins. AtDOA10A, but not the Brassicaceae-specific AtDOA10B, can compensate for loss of yeast ScDOA10 function. Transcriptome and Nt-acetylome profiling of an Atdoa10a/b RNAi mutant revealed no significant differences in the global NTA profile compared to wildtype, suggesting that AtDOA10s do not regulate the bulk turnover of NTA substrates. Using protein steady-state and cycloheximide-chase degradation assays in yeast and Arabidopsis, we show that turnover of ER-localised squalene epoxidase 1 (AtSQE1), a critical sterol biosynthesis enzyme, is mediated by AtDOA10s. Degradation of AtSQE1 in planta does not depend on NTA, but Nt-acetyltransferases indirectly impact its turnover in yeast, indicating kingdom-specific differences in NTA and cellular proteostasis. Our work suggests that, in contrast to yeast and mammals, targeting of Nt-acetylated proteins is not a major function of DOA10-like E3 ligases in Arabidopsis, and provides further insight into plant ERAD and the conservation of regulatory mechanisms controlling sterol biosynthesis in eukaryotes.
HostingRepository	PRIDE
AnnounceDate	2024-01-26
AnnouncementXML	Submission_2024-01-26_09:54:02.382.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Jean Baptiste BOYER
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	acetylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2023-06-22 15:07:03	ID requested
⏵ 1	2024-01-26 09:54:03	announced

10.1093/plphys/kiad406;

Etherington RD, Bailey M, Boyer JB, Armbruster L, Cao X, Coates JC, Meinnel T, Wirtz M, Giglione C, Gibbs DJ, Nt-acetylation-independent turnover of SQUALENE EPOXIDASE 1 by Arabidopsis DOA10-like E3 ligases. Plant Physiol, 193(3):2086-2104(2023) [pubmed]

submitter keyword: ERAD,Nt-acetylation, Ac/N-degron pathway, sterol biosynthesis, proteolysis, Ac/N-recognin, N-terminomics

Carmela GIGLIONE
contact affiliation	Protein Maturation, Cell fate and Therapeutics, Institute for Integrative Biology of the Cell (I2BC), CNRS UMR9198, Batiment 21, 1 Avenue de la Terrasse F-91198 Gif-sur-Yvette CEDEX, France
contact email	carmela.giglione@i2bc.paris-saclay.fr
lab head
Jean Baptiste BOYER
contact affiliation	Institut de Biologie Intégrative de la Cellule - CNRS
contact email	jean-baptiste.boyer@i2bc.paris-saclay.fr
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD043217
     1. Label: PRIDE project
     2. Name: Global and protein-specific analysis reveals Nt-acetylation-independent turnover of SQE1 by Arabidopsis DOA10-like E3 ligases