Conversion of the 2 Cl(-)/1 H(+) antiporter ClC-5 in a NO(3)(-)/H(+) antiporter by a single point mutation. (Articolo in rivista)

Type
Label
  • Conversion of the 2 Cl(-)/1 H(+) antiporter ClC-5 in a NO(3)(-)/H(+) antiporter by a single point mutation. (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1038/emboj.2008.284 (literal)
Alternative label
  • Giovanni Zifarelli; Michael Pusch (2009)
    Conversion of the 2 Cl(-)/1 H(+) antiporter ClC-5 in a NO(3)(-)/H(+) antiporter by a single point mutation.
    in EMBO journal (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Giovanni Zifarelli; Michael Pusch (literal)
Pagina inizio
  • 175 (literal)
Pagina fine
  • 182 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.nature.com/emboj/journal/v28/n3/full/emboj2008284a.html (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 28 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 3 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biofisica, CNR, Via De Marini, Genova, Italy (literal)
Titolo
  • Conversion of the 2 Cl(-)/1 H(+) antiporter ClC-5 in a NO(3)(-)/H(+) antiporter by a single point mutation. (literal)
Abstract
  • Several members of the CLC family are secondary active anion/proton exchangers, and not passive chloride channels. Among the exchangers, the endosomal ClC-5 protein that is mutated in Dent's disease shows an extreme outward rectification that precludes a precise determination of its transport stoichiometry from measurements of the reversal potential. We developed a novel imaging method to determine the absolute proton flux in Xenopus oocytes from the extracellular proton gradient. We determined a transport stoichiometry of 2 Cl(-)/1 H+. Nitrate uncoupled proton transport but mutating the highly conserved serine 168 to proline, as found in the plant NO3(-)/H+ antiporter atClCa, led to coupled NO3(-)/H+ exchange. Among several amino acids tested at position 168, S168P was unique in mediating highly coupled NO3(-)/H+ exchange. We further found that ClC-5 is strongly stimulated by intracellular protons in an allosteric manner with an apparent pK of approximately 7.2. A 2:1 stoichiometry appears to be a general property of CLC anion/proton exchangers. Serine 168 has an important function in determining anionic specificity of the exchange mechanism. (literal)
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