Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/24175
Type: Artigo de periódico
Title: Important amino acid residues of potato plant uncoupling protein (StUCP)
Author: Jezek, P.
Costa, A.D.T.
Vercesi, A.E.
Abstract: Chemical modifications were used to identify some of the functionally important amino acid residues of the potato plant uncoupling protein (StUCP). The proton-dependent swelling of potato mitochondria in K+-acetate in the presence of linoleic acid and valinomycin was inhibited by mersalyl (Ki = 5 µM) and other hydrophilic SH reagents such as Thiolyte MB, iodoacetate and 5,5'-dithio-bis-(2-nitrobenzoate), but not by hydrophobic N-ethylmaleimide. This pattern of inhibition by SH reagents was similar to that of brown adipose tissue uncoupling protein (UCP1). As with UCP1, the arginine reagent 2,3-butadione, but not N-ethylmaleimide or other hydrophobic SH reagents, prevented the inhibition of StUCP-mediated transport by ATP in isolated potato mitochondria or with reconstituted StUCP. The results indicate that the most reactive amino acid residues in UCP1 and StUCP are similar, with the exception of N-ethylmaleimide-reactive cysteines in the purine nucleotide-binding site.
Subject: plant mitochondria
uncoupling protein
chemical modification
mitochondrial swelling
reconstitution
Editor: Associação Brasileira de Divulgação Científica
Rights: aberto
Identifier DOI: 10.1590/S0100-879X2000001200003
Address: http://dx.doi.org/10.1590/S0100-879X2000001200003
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000001200003
Date Issue: 1-Dec-2000
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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