The proline 160 in the selectivity filter of the Arabidopsis NO(3)(-)/H(+) exchanger AtCLCa is essential for nitrate accumulation in planta (Articolo in rivista)

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  • The proline 160 in the selectivity filter of the Arabidopsis NO(3)(-)/H(+) exchanger AtCLCa is essential for nitrate accumulation in planta (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1111/j.1365-313X.2010.04288.x (literal)
Alternative label
  • Stefanie Wege, Mathieu Jossier, Sophie Filleur, Sébastien Thomine, Hélène Barbier-Brygoo, Franco Gambale, Alexis De Angeli (2010)
    The proline 160 in the selectivity filter of the Arabidopsis NO(3)(-)/H(+) exchanger AtCLCa is essential for nitrate accumulation in planta
    in Plant journal (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Stefanie Wege, Mathieu Jossier, Sophie Filleur, Sébastien Thomine, Hélène Barbier-Brygoo, Franco Gambale, Alexis De Angeli (literal)
Pagina inizio
  • 861 (literal)
Pagina fine
  • 869 (literal)
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  • http://onlinelibrary.wiley.com/doi/10.1111/j.1365-313X.2010.04288.x/abstract;jsessionid=224E9D4B1A62EDA7F8CC0E3CB07D9695.d03t01 (literal)
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  • 63 (literal)
Rivista
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  • 5 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institut des Sciences du Végétal, Centre National de la Recherche Scientifique , 1 Avenue de la Terrasse, 91198 Gif-Sur-Yvette Cedex Université Paris 7 Denis Diderot, Unité de Formation et de Recherche Sciences du Vivant, 35 rue Hélène Brion, 75205 Paris Cedex 13, France Istituto di Biofisica, Consiglio Nazionale delle Ricerche, Via De Marini 6, 16149 Genova, Italy (literal)
Titolo
  • The proline 160 in the selectivity filter of the Arabidopsis NO(3)(-)/H(+) exchanger AtCLCa is essential for nitrate accumulation in planta (literal)
Abstract
  • Nitrate, the major nitrogen source for plants, can be accumulated in the vacuole. Its transport across the vacuolar membrane is mediated by AtCLCa, an antiporter of the chloride channel (CLC) protein family. In contrast to other CLC family members, AtCLCa transports nitrate coupled to protons. Recently, the different behaviour towards nitrate of CLC proteins has been linked to the presence of a serine or proline in the selectivity filter motif GXGIP. By monitoring AtCLCa activity in its native environment, we show that if proline 160 in AtCLCa is changed to a serine (AtCLCaP160S), the transporter loses its nitrate selectivity, but the anion proton exchange mechanism is unaffected. We also performed in vivo analyses in yeast and Arabidopsis. In contrast to native AtCLCa, expression of AtCLCaP160S does not complement either the ?ScCLC yeast mutant grown on nitrate or the nitrate under-accumulation phenotype of clca knockout plants. Our results confirm the significance of this amino acid in the conserved selectivity filter of CLC proteins and highlight the importance of the proline in AtCLCa for nitrate metabolism in Arabidopsis. (literal)
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