JavaScript is disabled for your browser. Some features of this site may not work without it.

    Listar

    Todo RIUMAComunidades & ColeccionesPor fecha de publicaciónAutoresTítulosMateriasTipo de publicaciónCentrosDepartamentos/InstitutosEditoresEsta colecciónPor fecha de publicaciónAutoresTítulosMateriasTipo de publicaciónCentrosDepartamentos/InstitutosEditores

    Mi cuenta

    AccederRegistro

    Estadísticas

    Ver Estadísticas de uso

    DE INTERÉS

    Datos de investigaciónReglamento de ciencia abierta de la UMAPolítica de RIUMAPolitica de datos de investigación en RIUMAOpen Policy Finder (antes Sherpa-Romeo)Dulcinea
    Preguntas frecuentesManual de usoContacto/Sugerencias
    Ver ítem 
    •   RIUMA Principal
    • Investigación
    • Artículos
    • Ver ítem
    •   RIUMA Principal
    • Investigación
    • Artículos
    • Ver ítem

    The amino acid permease PpAAP1 mediates arginine transport in maritime pine.

    • Autor
      Llebrés, María Teresa; Castro-Rodríguez, Vanessa Viviana; Pascual-Moreno, María BelénAutoridad Universidad de Málaga; Ávila-Sáez, ConcepciónAutoridad Universidad de Málaga; Cánovas-Ramos, Francisco MiguelAutoridad Universidad de Málaga
    • Fecha
      2021
    • Editorial/Editor
      Oxford University Press
    • Palabras clave
      Genética forestal; Arginina; Pino marítimo
    • Resumen
      Forest trees have access to diverse nitrogenous compounds in the soil such as ammonium, nitrate and amino acids. Recent progress has been made in the identification and characterization of ammonium and nitrate transporters. However, much more limited is our current knowledge of amino acid transport systems despite their relevance to fully understanding nitrogen nutrition in trees. In the present study, we have identified 10 genes encoding putative amino acid permeases of the AAP family in maritime pine (Pinus pinaster Ait.). Four members of this family, PpAAP1, PpAAP2, PpAAP3 and PpAAP4 were phylogenetically related to AtAAP5, involved in arginine transport in Arabidopsis thaliana. One of these genes, PpAAP1, exhibited enhanced expression levels in maritime pine roots when arginine was externally supplied. PpAAP1 was functionally characterized by complementation of a yeast mutant strain defective in the transport of arginine, allowing yeast to take up [14C]-arginine with high affinity. Furthermore, PpAAP1 was able to restore the severely affected root uptake of arginine displayed by AtAAP5 T-DNA mutants. Uptake rates of 15N-labelled arginine were significantly higher in PpAAP1-overexpressing plants when compared to wild-type and AtAAP5 mutant plants. Taken together, our results indicate that PpAAP1 is a high-affinity arginine transporter in maritime pine.
    • URI
      https://hdl.handle.net/10630/37933
    • DOI
      https://dx.doi.org/10.1093/treephys/tpab089
    • Compartir
      RefworksMendeley
    Mostrar el registro completo del ítem
    Ficheros
    PpAAP1SUBBMISSION_JULIO2021.pdf (3.504Mb)
    Colecciones
    • Artículos

    Estadísticas

    REPOSITORIO INSTITUCIONAL UNIVERSIDAD DE MÁLAGA
    REPOSITORIO INSTITUCIONAL UNIVERSIDAD DE MÁLAGA
     

     

    REPOSITORIO INSTITUCIONAL UNIVERSIDAD DE MÁLAGA
    REPOSITORIO INSTITUCIONAL UNIVERSIDAD DE MÁLAGA