Cotranslational N-degron masking by acetylation promotes proteome stability in plants

Eric Linster, Francy L. Forero Ruiz, Pavlina Miklankova, Thomas Ruppert, Johannes Mueller, Laura Armbruster, Xiaodi Gong, Giovanna Serino, Matthias Mann, Rüdiger Hell and Markus Wirtz ()
Additional contact information
Eric Linster: Heidelberg University
Francy L. Forero Ruiz: Heidelberg University
Pavlina Miklankova: Heidelberg University
Thomas Ruppert: Heidelberg University
Johannes Mueller: Max-Planck-Institute for Biochemistry
Laura Armbruster: Heidelberg University
Xiaodi Gong: Heidelberg University
Giovanna Serino: Sapienza Università di Roma
Matthias Mann: Max-Planck-Institute for Biochemistry
Rüdiger Hell: Heidelberg University
Markus Wirtz: Heidelberg University

Nature Communications, 2022, vol. 13, issue 1, 1-12

Abstract: Abstract N-terminal protein acetylation (NTA) is a prevalent protein modification essential for viability in animals and plants. The dominant executor of NTA is the ribosome tethered Nα-acetyltransferase A (NatA) complex. However, the impact of NatA on protein fate is still enigmatic. Here, we demonstrate that depletion of NatA activity leads to a 4-fold increase in global protein turnover via the ubiquitin-proteasome system in Arabidopsis. Surprisingly, a concomitant increase in translation, actioned via enhanced Target-of-Rapamycin activity, is also observed, implying that defective NTA triggers feedback mechanisms to maintain steady-state protein abundance. Quantitative analysis of the proteome, the translatome, and the ubiquitome reveals that NatA substrates account for the bulk of this enhanced turnover. A targeted analysis of NatA substrate stability uncovers that NTA absence triggers protein destabilization via a previously undescribed and widely conserved nonAc/N-degron in plants. Hence, the imprinting of the proteome with acetylation marks is essential for coordinating proteome stability.

Date: 2022
References: View references in EconPapers View complete reference list from CitEc
Citations: View citations in EconPapers (8)

Downloads: (external link)
https://www.nature.com/articles/s41467-022-28414-5 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-28414-5

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-022-28414-5

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().