Functional characterization of residues within the carnitine/acylcarnitine translocase RX(2)PANAAXF distinct motif (Articolo in rivista)

Type
Label
  • Functional characterization of residues within the carnitine/acylcarnitine translocase RX(2)PANAAXF distinct motif (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Alternative label
  • De Lucas JR; Indiveri C; Tonazzi A; Perez P; Giangregorio N; Iacobazzi V;Palmieri F (2008)
    Functional characterization of residues within the carnitine/acylcarnitine translocase RX(2)PANAAXF distinct motif
    in Molecular membrane biology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • De Lucas JR; Indiveri C; Tonazzi A; Perez P; Giangregorio N; Iacobazzi V;Palmieri F (literal)
Pagina inizio
  • 152 (literal)
Pagina fine
  • 163 (literal)
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  • 25 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Departamento de Microbiología y Parasitología, Facultad de Farmacia, Campus Universitario, Universidad de Alcalá, Alcalá de Henares, Madrid, Spain Department of Cellular Biology, University of Calabria, Via P.Bucci cubo 4c, 87036 Arcavacata di Rende (CS), Italy National Research Council Institute of Biomembranes and Bioenergetics (IBBE), via Amendola 165/A, 70126, Bari, Italy Laboratory of Biochemistry and Molecular Biology, Department of Pharmaco-Biology, University of Bari, Via Orabona 4, 70125 Bari, Italy (literal)
Titolo
  • Functional characterization of residues within the carnitine/acylcarnitine translocase RX(2)PANAAXF distinct motif (literal)
Abstract
  • presence of a distinct motif, RXXPANAAXF, within its sixth transmembrane alpha-helix. In this study, we analysed the role of the amino acids of this motif in the structure-function relationships of the human CAC by using two complementary approaches. First, we performed functional analysis in the model fungus Aspergillus nidulans of selected mutations with structural and functional relevance. Second, similar mutant human CACs were biochemically characterized after their reconstitution into liposomes. Both analyses have provided relevant information on the importance and role of the CAC motif residues in the activity and metabolic function of CAC. Only the two adjacent alanines, Ala281 and Ala282 in the human CAC, have been found not to be crucial for transport activity and in vivo function. Results obtained from amino acid substitutions of residues Arg275, Asn280 and Phe284 of human CAC together with structural analysis using molecular modelling of the carrier suggest that R275, N280 and F284 are involved in substrate binding during acylcarnitine/carnitine translocation. Furthermore, functional analysis of mutations of residues Pro278 and Ala279 in A. nidulans, t (literal)
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