Report
Revisiting the functional properties of NPF6.3/NRT1.1/CHL1 in xenopus oocytes
| العنوان: | Revisiting the functional properties of NPF6.3/NRT1.1/CHL1 in xenopus oocytes |
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| المؤلفون: | Noguero, Mélanie, Léran, Sophie, Bouguyon, Éléonore, Brachet, Chantal, Tillard, Pascal, Nacry, Philippe, Gojon, Alain, Krouk, Gabriel, Lacombe, Benoît |
| المساهمون: | Biochimie et Physiologie Moléculaire des Plantes (BPMP), Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), This work was supported by the Institut National de la Recherche Agronomique (CJS PhD Fellowship to SL & Projet Département BAP, BAP2013-33-NITSE to BL), and the Région Languedoc-Roussillon (Chercheur d’Avenir to BL)., ANR-11-JSV6-0002,NUTSE,Perception des nutriments chez les plantes(2011), ANR-14-CE34-0007,HONIT,Hormone cross-talk drives nutrient dependent plant development(2014) |
| المصدر: | https://hal.science/hal-01777543 ; 2018. |
| بيانات النشر: | CCSD |
| سنة النشر: | 2018 |
| مصطلحات موضوعية: | xenopus oocyte, transporteur de nitrate, transport d'auxine, patch clamp, arabidopsis, [SDV]Life Sciences [q-bio] |
| الوصف: | preprint déposé dans bioRxiv ; Within the Arabidopsis NPF proteins, most of the characterized nitrate transporters are low-affinity transporters, whereas the functional characterization of NPF6.3/NRT1.1 has revealed interesting transport properties: the transport of nitrate and auxin, the eletrogenicity of the nitrate transport and a dual-affinity transport behavior for nitrate depending on external nitrate concentration. However, some of these properties remained controversial and were challenged here. We functionally express WT NPF6.3/NRT1.1 and some of its mutant in Xenopus oocytes and used a combination of uptake experiments using 15N-labelled nitrate and two-electrode voltage-clamp. In our experimental conditions in xenopus oocytes, in the presence or in the absence of external chloride, NPF6.3/NRT1.1 behaves as a non- electrogenic and pure low-affinity transporter. Moreover, further functional characterization of a NPF6.3/NRT1.1 point mutant, P492L, allowed us to hypothesize that NPF6.3/NRT1.1 is regulated by internal nitrate concentration and that the internal perception site involves the P492 residue. |
| نوع الوثيقة: | report |
| اللغة: | English |
| Relation: | BIORXIV: 244467; PRODINRA: 427610 |
| DOI: | 10.1101/244467 |
| الاتاحة: | https://hal.science/hal-01777543 https://hal.science/hal-01777543v1/document https://hal.science/hal-01777543v1/file/NogueroM-et%20al-BioRxiv-2018.pdf https://doi.org/10.1101/244467 |
| Rights: | http://creativecommons.org/licenses/by-nc-nd/ ; info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: | edsbas.B902C4F0 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1101/244467 |
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