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| Verfasst von: | Gong, Xiaodi [VerfasserIn]  |
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| | Boyer, Jean-Baptiste [VerfasserIn] |
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| | Gierlich, Simone [VerfasserIn] |
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| | Pożoga, Marlena [VerfasserIn] |
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| | Weidenhausen, Jonas [VerfasserIn] |
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| | Sinning, Irmgard [VerfasserIn] |
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| | Meinnel, Thierry [VerfasserIn] |
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| | Giglione, Carmela [VerfasserIn] |
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| | Wang, Yonghong [VerfasserIn] |
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| | Hell, Rüdiger [VerfasserIn] |
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| | Wirtz, Markus [VerfasserIn] |
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| Titel: | HYPK controls stability and catalytic activity of the N-terminal acetyltransferase A in Arabidopsis thaliana |
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| Verf.angabe: | Xiaodi Gong, Jean-Baptiste Boyer, Simone Gierlich, Marlena Pożoga, Jonas Weidenhausen, Irmgard Sinning, Thierry Meinnel, Carmela Giglione, Yonghong Wang, Rüdiger Hell, and Markus Wirtz |
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| E-Jahr: | 2024 |
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| Jahr: | 27 February 2024 |
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| Umfang: | 20 S. |
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| Illustrationen: | Illustrationen |
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| Fussnoten: | Online verfügbar: 15. Februar 2024 ; Gesehen am 30.07.2024 |
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| Titel Quelle: | Enthalten in: Cell reports |
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| Ort Quelle: | Maryland Heights, MO : Cell Press, 2012 |
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| Jahr Quelle: | 2024 |
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| Band/Heft Quelle: | 43(2024), 2 vom: Feb., Artikel-ID 113768, Seite 1-20 |
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| ISSN Quelle: | 2211-1247 |
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| Abstract: | 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. |
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| DOI: | doi:10.1016/j.celrep.2024.113768 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
kostenfrei: Volltext: https://doi.org/10.1016/j.celrep.2024.113768 |
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| | kostenfrei: Volltext: https://www.sciencedirect.com/science/article/pii/S2211124724000962 |
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| | DOI: https://doi.org/10.1016/j.celrep.2024.113768 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | co-translational protein modification |
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| | drought resistance |
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| | HYPK |
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| | N-terminal acetylation |
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| | NatA |
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| | proteostasis |
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| K10plus-PPN: | 1896920195 |
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| Verknüpfungen: | → Zeitschrift |
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HYPK controls stability and catalytic activity of the N-terminal acetyltransferase A in Arabidopsis thaliana / Gong, Xiaodi [VerfasserIn]; 27 February 2024 (Online-Ressource)
