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dc.contributor.authorHegardt, Fausto G.-
dc.contributor.authorBach-Elias, Montse-
dc.contributor.authorAsins, Guillermina-
dc.contributor.authorCaudevilla, Concha-
dc.contributor.authorMorillas, M.-
dc.contributor.authorCodony, Carles-
dc.contributor.authorSerra, Dolors-
dc.date.accessioned2015-01-09T08:11:06Z-
dc.date.available2015-01-09T08:11:06Z-
dc.date.issued2001-05-
dc.identifier.citationBiochemical Society Transactions 29(2): 316–319 (2001)es_ES
dc.identifier.issn0300-5127-
dc.identifier.urihttp://hdl.handle.net/10261/109197-
dc.description672nd Meeting held at the University of Sussex, 19–21 December 2000 Speaker Manuscriptes_ES
dc.description.abstractCarnitine octanoyltransferase (COT) produces three different transcripts in rat through cis- and trans-splicing reactions, which can lead to the synthesis of two proteins. The occurrence of the three COT transcripts in rat has been found in all tissues examined and does not depend on sex, fat feeding, peroxisome proliferators or hyperinsulinaemia. Rat COT exon 2 contains a putative exonic splicing enhancer (ESE) sequence. Mutation of this ESE (GAAGAAG) to AAAAAAA decreased trans-splicing in vitro, from which it is deduced that this ESE sequence is partly responsible for the formation of the three transcripts. The protein encoded by cis-spliced mRNA of rat COT is inhibited by malonyl-CoA and etomoxir. cDNA species encoding full-length wild-type COT and one double mutant COT were expressed in Saccharomyces cerevisiae. The recombinant enzymes showed full activity towards both substrates, carnitine and decanoyl-CoA. The activity of the doubly mutated H131A/H340A enzyme was similar to that of the rat peroxisomal enzyme but was completely insensitive to malonyl-CoA and etomoxir. These results indicate that the histidine residues His-131 and His-340 are the sites responsible for the interaction of these two inhibitors, which inhibit COT by interacting with the same sites.es_ES
dc.description.sponsorshipThis study was supported by grant PB95-0012 from the Dirección General de Investigación Científica y Técnica, Spain, by an Ajut de Suport als Grups de Recerca de Catalunya, 1999SGR-0075 (to F. G. H.) and by a grant from the Fundació de la Marató de TV3. M. M. is a recipient of a fellowship from the Ministerio de Educación y Cultura, Dirección General de Enseñanza Superior, Spain.es_ES
dc.language.isoenges_ES
dc.publisherPortland Presses_ES
dc.rightsclosedAccesses_ES
dc.subjectEtomoxires_ES
dc.subjectExonic splicing enhancerses_ES
dc.subjectMalonyl-CoAes_ES
dc.subjectTrans-splicinges_ES
dc.titlePost-transcriptional regulation of rat carnitine octanoyltransferasees_ES
dc.typeartículoes_ES
dc.identifier.doi10.1042/bst0290316-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1042/bst0290316-
dc.identifier.e-issn1470-8752-
dc.contributor.funderDirección General de Investigación Científica y Técnica, DGICT (España)-
dc.contributor.funderGeneralitat de Catalunya-
dc.contributor.funderFundació La Marató de TV3-
dc.contributor.funderMinisterio de Educación y Cultura (España)-
dc.relation.csices_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100002809es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/100008666es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100008737es_ES
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