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Authordc.contributor.authorAraya Flores, Jorge 
Authordc.contributor.authorMiranda, Simon 
Authordc.contributor.authorCovarrubias Becerra, María Paz 
Authordc.contributor.authorStange Klein, Claudia 
Authordc.contributor.authorHandford, Michael 
Admission datedc.date.accessioned2020-06-18T20:52:02Z
Available datedc.date.available2020-06-18T20:52:02Z
Publication datedc.date.issued2020
Cita de ítemdc.identifier.citationPlant Physiol Biochem Volume: 151 Pages: 264-270 Jun 2020es_ES
Identifierdc.identifier.other10.1016/j.plaphy.2020.03.031
Identifierdc.identifier.urihttp://repositorio.uchile.cl/handle/2250/175574
Abstractdc.description.abstractLipoic acid (LA) and its reduced form (dihydrolipoic acid, DHLA) have unique antioxidant properties among such molecules. Moreover, after a process termed lipoylation, LA is an essential prosthetic group covalently-attached to several key multi-subunit enzymatic complexes involved in primary metabolism, including E2 subunits of pyruvate dehydrogenase (PDH). The metabolic pathway of lipoylation has been extensively studied in Escherichia coll. and Arabidopsis thaliana in which protein modification occurs via two routes: de novo synthesis and salvage. Common to both pathways, lipoyl synthase (LIP1 in plants, LipA in bacteria, EC 2.8.1.8) inserts sulphur atoms into the molecule in a final, activating step. However, despite the detection of LA and DHLA in other plant species, including tomato (Solanum lycopersicum), no plant LIP1s have been characterised to date from species other than Arabidopsis. In this work, we present the identification and characterisation of two LIPs from tomato, S1LIP1 and S1LIP1p. Consistent with in silico data, both are widely-expressed, particularly in reproductive organs. In line with bioinformatic predictions, we determine that yellow fluorescent protein tagged versions of S1LIP1 and S1LIP1p are mitochondrially- and plastidially-localised, respectively. Both possess the molecular hallmarks and domains of well-characterised bacterial LipAs. When heterologously-expressed in an E. coli lipA mutant, both are capable of complementing specific growth phenotypes and increasing lipoylation levels of E2 subunits of PDH in vivo, demonstrating that they do indeed function as lipoyl synthases.es_ES
Patrocinadordc.description.sponsorshipComisión Nacional de Investigación Cientifica y Tecnológica (CONICYT) CONICYT FONDECYT 1181198 Comisión Nacional de Investigación Cientifica y Tecnológica (CONICYT) PIA ACT192073 CONICYT Beca de Magíster Nacional 22151178 CONICYT Beca de Doctorado Nacional 21160916 Fundación María Ghilardi Venegas Fundación María Ghilardi Venegas scholarship Faculty of Sciences, Universidad de Chilees_ES
Lenguagedc.language.isoenes_ES
Publisherdc.publisherElsevieres_ES
Sourcedc.sourcePlant Physiology and Biochemistryes_ES
Títulodc.titleSolanum lycopersicum (tomato) possesses mitochondrial and plastidial lipoyl synthases capable of increasing lipoylation levels when expressed in bacteriaes_ES
Document typedc.typeArtículo de revistaes_ES
Catalogueruchile.catalogadorctces_ES
Indexationuchile.indexArtículo de publicación ISIes_ES
Access notedct.AccessRightsSin acceso a texto completoes_ES


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