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Verfasst von:Haas, Florian Heinrich [VerfasserIn]   i
 Heeg, Corinna [VerfasserIn]   i
 Wirtz, Markus [VerfasserIn]   i
 Hell, Rüdiger [VerfasserIn]   i
Titel:Mitochondrial serine Acetyltransferase functions as a pacemaker of cysteine synthesis in plant cells
Verf.angabe:Florian H. Haas, Corinna Heeg, Rafael Queiroz, Andrea Bauer, Markus Wirtz and Rüdiger Hell
E-Jahr:2008
Jahr:August 27, 2008
Umfang:13 S.
Fussnoten:Gesehen am 16.05.2017
Titel Quelle:Enthalten in: Plant physiology
Ort Quelle:Oxford : Oxford University Press, 1926
Jahr Quelle:2008
Band/Heft Quelle:148(2008), 2, Seite 1055-1067
ISSN Quelle:1532-2548
Abstract:Cysteine (Cys) synthesis in plants is carried out by two sequential reactions catalyzed by the rate-limiting enzyme serine acetyltransferase (SAT) and excess amounts of O-acetylserine(thiol)lyase. Why these reactions occur in plastids, mitochondria, and cytosol of plants remained unclear. Expression of artificial microRNA (amiRNA) against Sat3 encoding mitochondrial SAT3 in transgenic Arabidopsis (Arabidopsis thaliana) plants demonstrates that mitochondria are the most important compartment for the synthesis of O-acetylserine (OAS), the precursor of Cys. Reduction of RNA levels, protein contents, SAT enzymatic activity, and phenotype strongly correlate in independent amiSAT3 lines and cause significantly retarded growth. The expression of the other four Sat genes in the Arabidopsis genome are not affected by amiRNA-SAT3 according to quantitative real-time polymerase chain reaction and microarray analyses. Application of radiolabeled serine to leaf pieces revealed severely reduced incorporation rates into Cys and even more so into glutathione. Accordingly, steady-state levels of OAS are 4-fold reduced. Decrease of sulfate reduction-related genes is accompanied by an accumulation of sulfate in amiSAT3 lines. These results unequivocally show that mitochondria provide the bulk of OAS in the plant cell and are the likely site of flux regulation. Together with recent data, the cytosol appears to be a major site of Cys synthesis, while plastids contribute reduced sulfur as sulfide. Thus, Cys synthesis in plants is significantly different from that in nonphotosynthetic eukaryotes at the cellular level.
DOI:doi:10.1104/pp.108.125237
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: http://dx.doi.org/10.1104/pp.108.125237
 kostenfrei: Volltext: https://academic.oup.com/plphys/article/148/2/1055/6107496
 DOI: https://doi.org/10.1104/pp.108.125237
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:155868347X
Verknüpfungen:→ Zeitschrift

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