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Verfasst von:Linster, Eric [VerfasserIn]   i
 Forero Ruiz, Francy Liliana [VerfasserIn]   i
 Miklánková, Pavlína [VerfasserIn]   i
 Ruppert, Thomas [VerfasserIn]   i
 Mueller, Johannes [VerfasserIn]   i
 Armbruster, Laura [VerfasserIn]   i
 Gong, Xiaodi [VerfasserIn]   i
 Serino, Giovanna [VerfasserIn]   i
 Mann, Matthias [VerfasserIn]   i
 Hell, Rüdiger [VerfasserIn]   i
 Wirtz, Markus [VerfasserIn]   i
Titel:Cotranslational N-degron masking by acetylation promotes proteome stability in plants
Verf.angabe:Eric Linster, Francy L. Forero Ruiz, Pavlina Miklankova, Thomas Ruppert, Johannes Mueller, Laura Armbruster, Xiaodi Gong, Giovanna Serino, Matthias Mann, Rüdiger Hell & Markus Wirtz
E-Jahr:2022
Jahr:10 February 2022
Umfang:12 S.
Fussnoten:Gesehen am 30.03.2022
Titel Quelle:Enthalten in: Nature Communications
Ort Quelle:[London] : Nature Publishing Group UK, 2010
Jahr Quelle:2022
Band/Heft Quelle:13(2022), Artikel-ID 810, Seite 1-12
ISSN Quelle:2041-1723
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.
DOI:doi:10.1038/s41467-022-28414-5
URL:kostenfrei: Volltext: https://doi.org/10.1038/s41467-022-28414-5
 kostenfrei: Volltext: https://www.nature.com/articles/s41467-022-28414-5
 DOI: https://doi.org/10.1038/s41467-022-28414-5
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Plant stress responses
 Proteomics
 Ubiquitylation
K10plus-PPN:1796012475
Verknüpfungen:→ Zeitschrift
 
 
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