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Status: Bibliographieeintrag

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Verfasst von:Pożoga, Marlena [VerfasserIn]   i
 Armbruster, Laura [VerfasserIn]   i
 Wirtz, Markus [VerfasserIn]   i
Titel:From nucleus to membrane
Titelzusatz:a subcellular map of the N-acetylation machinery in plants
Verf.angabe:Marlena Pożoga, Laura Armbruster and Markus Wirtz
E-Jahr:2022
Jahr:21 November 2022
Umfang:22 S.
Fussnoten:Gesehen am 31.01.2023
Titel Quelle:Enthalten in: International journal of molecular sciences
Ort Quelle:Basel : Molecular Diversity Preservation International, 2000
Jahr Quelle:2022
Band/Heft Quelle:23(2022), 22, Artikel-ID 14492, Seite 1-22
ISSN Quelle:1422-0067
 1661-6596
Abstract:N-terminal acetylation (NTA) is an ancient protein modification conserved throughout all domains of life. N-terminally acetylated proteins are present in the cytosol, the nucleus, the plastids, mitochondria and the plasma membrane of plants. The frequency of NTA differs greatly between these subcellular compartments. While up to 80% of cytosolic and 20-30% of plastidic proteins are subject to NTA, NTA of mitochondrial proteins is rare. NTA alters key characteristics of proteins such as their three-dimensional structure, binding properties and lifetime. Since the majority of proteins is acetylated by five ribosome-bound N-terminal acetyltransferases (Nats) in yeast and humans, NTA was long perceived as an exclusively co-translational process in eukaryotes. The recent characterization of post-translationally acting plant Nats, which localize to the plasma membrane and the plastids, has challenged this view. Moreover, findings in humans, yeast, green algae and higher plants uncover differences in the cytosolic Nat machinery of photosynthetic and non-photosynthetic eukaryotes. These distinctive features of the plant Nat machinery might constitute adaptations to the sessile lifestyle of plants. This review sheds light on the unique role of plant N-acetyltransferases in development and stress responses as well as their evolution-driven adaptation to function in different cellular compartments.
DOI:doi:10.3390/ijms232214492
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.

Volltext: https://doi.org/10.3390/ijms232214492
 Volltext: https://www.mdpi.com/1422-0067/23/22/14492
 DOI: https://doi.org/10.3390/ijms232214492
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:co-translational modification
 compartmentalization
 GNAT
 N-terminal acetylation
 protein turnover
 PTM
 stress responses
K10plus-PPN:183274230X
Verknüpfungen:→ Zeitschrift

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