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Verfasst von:Lescano, Ignacio [VerfasserIn]   i
 Bogino, María Florencia [VerfasserIn]   i
 Martini, Carolina [VerfasserIn]   i
 Tessi, Tomás María [VerfasserIn]   i
 González, Claudio Alejandro [VerfasserIn]   i
 Schumacher, Karin [VerfasserIn]   i
 Desimone, Marcelo [VerfasserIn]   i
Titel:Ureide permease 5 (AtUPS5) connects cell compartments involved in ureide metabolism
Verf.angabe:Ignacio Lescano, María Florencia Bogino, Carolina Martini, Tomás María Tessi, Claudio Alejandro González, Karin Schumacher, and Marcelo Desimone
E-Jahr:2020
Jahr:[March 2020]
Umfang:16 S.
Fussnoten:Gesehen am 09.04.2020
Titel Quelle:Enthalten in: Plant physiology
Ort Quelle:Rockville, Md. : Soc., 1926
Jahr Quelle:2020
Band/Heft Quelle:182(2020), 3, Seite 1310-1325
ISSN Quelle:1532-2548
Abstract:Allantoin is a purine oxidative product involved in long distance transport of organic nitrogen in nodulating legumes and was recently shown to play a role in stress tolerance in other plants. The subcellular localization of enzymes that catalyze allantoin synthesis and degradation indicates that allantoin is produced in peroxisomes and degraded in the endoplasmic reticulum (ER). Although it has been determined that allantoin is mostly synthesized in roots and transported to shoots either for organic nitrogen translocation in legumes or for plant protection during stress in Arabidopsis (Arabidopsis thaliana), the mechanism and molecular components of allantoin export from root cells are still unknown. AtUPS5 (Arabidopsis UREIDE PERMEASE 5) is a transmembrane protein that transports allantoin with high affinity when expressed in yeast. The subcellular fate of splicing variants AtUPS5L (long) and AtUPS5S (short) was studied by tagging them with fluorescent proteins in their cytosolic loops. The capability of these fusion proteins to complement the function of the native proteins was demonstrated by nutritional and salt stress experiments. Both variants localized to the ER, but the AtUPS5L variant was also detected in the trans-Golgi network/early endosome and at the plasma membrane. AtUPS5L and AtUPS5S localization indicates that they could have different roles in allantoin distribution between subcellular compartments. Our data suggest that under nonstress conditions UPS5L and UPS5S may function in allantoin degradation for nutrient recycling, whereas under stress, both genes may be involved in vesicular export allowing allantoin translocation from roots to shoots.
DOI:doi:10.1104/pp.19.01136
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 ; Verlag: https://doi.org/10.1104/pp.19.01136
 Volltext: http://www.plantphysiol.org/content/182/3/1310
 DOI: https://doi.org/10.1104/pp.19.01136
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1694349365
Verknüpfungen:→ Zeitschrift

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