PXD047700-1

PXD047700 is an original dataset announced via ProteomeXchange.

Title	HYPK controls stability and catalytic activity of the N-terminal acetyltransferase A in Arabidopsis thaliana
Description	The ribosome-tethered N-terminal acetyltransferase A (NatA) acetylates 52% of soluble proteins in Arabidopsis thaliana. This co-translational shielding of the N-terminus stabilizes diverse cytosolic plant proteins. The Huntingtin yeast partner K (HYPK) facilitates NatA activity in planta, but in vitro, the N-terminal a-helix1 of HYPK inhibits NatA in the ternary NatA/HYPK complex. Consequently, the mechanism of HYPK function in plants was unknown. To understand the regulatory function of HYPK at the molecular level, we genetically engineered CRISPR/Cas9 mutants expressing either a non-functional HYPK (hypk-cr1) or an N-terminally deleted HYPK version (hypk-cr2). Like NatA-activity-depleted mutants, the hypk-cr1 and –cr2 mutants were more tolerant to drought stress and suffered from global proteome destabilization. Surprisingly, we found that absence of HYPK led to destabilization of the NatA subunits in leaves but not in roots of hypk-cr1. Further genetic and molecular evidence demonstrated that the stability of NatA subunits in leaves is mainly controlled by the C-terminal UBA domain of HYPK. While retaining the UBA domain, NatA activity was still impaired in hypk-cr2 leaves, implying that the N terminus of HYPK also contributes to the regulation of NatA activity. Furthermore, crossing of hypk-cr1 with a NatA-depleted mutant uncovered that HYPK promotes NatA activity not only by stabilizing NatA. Taken together, the activity-promoting function of the HYPK N-terminus depends on the binding of HYPK to NatA via the UBA domain, and is critical for NatA substrates starting with various amino acids. Our findings improve our understanding of the NatA regulatory subunit HYPK.
HostingRepository	PRIDE
AnnounceDate	2024-01-22
AnnouncementXML	Submission_2024-01-22_01:40:33.496.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	2023-12-11 02:26:07	ID requested
⏵ 1	2024-01-22 01:40:33	announced

Dataset with its publication pending

submitter keyword: co-translational protein modification,N-terminal acetylation, NatA, HYPK, drought resistance

Dr Carmela GIGLIONE
contact affiliation	Protein Maturation, Cell fate and Therapeutics, Institute for Integrative Biology of the Cell (I2BC), CNRS UMR9198, Bâtiment 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. PXD047700
     1. Label: PRIDE project
     2. Name: HYPK controls stability and catalytic activity of the N-terminal acetyltransferase A in Arabidopsis thaliana