Cover Image

HYPK controls stability and catalytic activity of the N-terminal acetyltransferase A in Arabidopsis thaliana

The ribosome-tethered N-terminal acetyltransferase A (NatA) acetylates 52% of soluble proteins in Arabidopsis thaliana. This co-translational modification of the N terminus stabilizes diverse cytosolic plant proteins. The evolutionary conserved Huntingtin yeast partner K (HYPK) facilitates NatA acti...

Full description

Saved in:
Bibliographic Details
Main Authors: Gong, Xiaodi (Author) , Boyer, Jean-Baptiste (Author) , Gierlich, Simone (Author) , Pożoga, Marlena (Author) , Weidenhausen, Jonas (Author) , Sinning, Irmgard (Author) , Meinnel, Thierry (Author) , Giglione, Carmela (Author) , Wang, Yonghong (Author) , Hell, Rüdiger (Author) , Wirtz, Markus (Author)
Format: Article (Journal)
Language:English
Published: 27 February 2024
In: Cell reports
Year: 2024, Volume: 43, Issue: 2, Pages: 1-20
ISSN:2211-1247
DOI:10.1016/j.celrep.2024.113768
Online Access:Verlag, kostenfrei, Volltext: https://doi.org/10.1016/j.celrep.2024.113768
Verlag, kostenfrei, Volltext: https://www.sciencedirect.com/science/article/pii/S2211124724000962
Get full text
Author Notes:Xiaodi Gong, Jean-Baptiste Boyer, Simone Gierlich, Marlena Pożoga, Jonas Weidenhausen, Irmgard Sinning, Thierry Meinnel, Carmela Giglione, Yonghong Wang, Rüdiger Hell, and Markus Wirtz
Description
Summary:The ribosome-tethered N-terminal acetyltransferase A (NatA) acetylates 52% of soluble proteins in Arabidopsis thaliana. This co-translational modification of the N terminus stabilizes diverse cytosolic plant proteins. The evolutionary conserved Huntingtin yeast partner K (HYPK) facilitates NatA activity in planta, but in vitro, its N-terminal helix α1 inhibits human NatA activity. To dissect the regulatory function of HYPK protein domains in vivo, we genetically engineer CRISPR-Cas9 mutants expressing a HYPK fragment lacking all functional domains (hypk-cr1) or an internally deleted HYPK variant truncating helix α1 but retaining the C-terminal ubiquitin-associated (UBA) domain (hypk-cr2). We find that the UBA domain of HYPK is vital for stabilizing the NatA complex in an organ-specific manner. The N terminus of HYPK, including helix α1, is critical for promoting NatA activity on substrates starting with various amino acids. Consequently, deleting only 42 amino acids inside the HYPK N terminus causes substantial destabilization of the plant proteome and higher tolerance toward drought stress.
Item Description:Online verfügbar: 15. Februar 2024
Gesehen am 30.07.2024
Physical Description:Online Resource
ISSN:2211-1247
DOI:10.1016/j.celrep.2024.113768

Similar Items