ATP binding to the C-terminus of the Arabidopsis thaliana, AtCLCa, regulates nitrate transport into plant vacuoles. (Articolo in rivista)

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  • ATP binding to the C-terminus of the Arabidopsis thaliana, AtCLCa, regulates nitrate transport into plant vacuoles. (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1074/jbc.M109.005132 (literal)
Alternative label
  • De Angeli A.; Moran O.; Wege S.; Filleur S.; Ephritikhine G.; Thomine S.; Barbier-Brygoo H.; Gambale F. (2009)
    ATP binding to the C-terminus of the Arabidopsis thaliana, AtCLCa, regulates nitrate transport into plant vacuoles.
    in The Journal of biological chemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • De Angeli A.; Moran O.; Wege S.; Filleur S.; Ephritikhine G.; Thomine S.; Barbier-Brygoo H.; Gambale F. (literal)
Pagina inizio
  • 26526 (literal)
Pagina fine
  • 26532 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.jbc.org/content/284/39/26526 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 284 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 39 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biofisica, Consiglio Nazionale delle Ricerche, Via De Marini 6, 16149 Genova, Italy Institut des Sciences du Végétal, CNRS, 1 Avenue de la Terrasse, 91198 Gif-Sur-Yvette Cedex, France Université Paris 7-Denis Diderot, UFR Sciences du Vivant, 35 rue Hélène Brion, 75205 Paris Cedex 13, France (literal)
Titolo
  • ATP binding to the C-terminus of the Arabidopsis thaliana, AtCLCa, regulates nitrate transport into plant vacuoles. (literal)
Abstract
  • Nitrate, one of the major nitrogen sources for plants, is stored in the vacuole. Nitrate accumulation within the vacuole is primarily mediated by the NO(3)(-)/H(+) exchanger AtCLCa, which belongs to the chloride channel (CLC) family. Crystallography analysis of hCLC5 suggested that the C-terminal domain, composed by two cystathionine beta-synthetase motifs in all eukaryotic members of the CLC family is able to interact with ATP. However, interaction of nucleotides with a functional CLC protein has not been unambiguously demonstrated. Here we show that ATP reversibly inhibits AtCLCa by interacting with the C-terminal domain. Applying the patch clamp technique to isolated Arabidopsis thaliana vacuoles, we demonstrate that ATP reduces AtCLCa activity with a maximum inhibition of 60%. ATP inhibition of nitrate influx into the vacuole at cytosolic physiological nitrate concentrations suggests that ATP modulation is physiologically relevant. ADP and AMP do not decrease the AtCLCa transport activity; nonetheless, AMP (but not ADP) competes with ATP, preventing inhibition. A molecular model of the C terminus of AtCLCa was built by homology to hCLC5 C terminus. The model predicted the effects of mutations of the ATP binding site on the interaction energy between ATP and AtCLCa that were further confirmed by functional expression of site-directed mutated AtCLCa. (literal)
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