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Solanum lycopersicum (tomato) possesses mitochondrial and plastidial lipoyl synthases capable of increasing lipoylation levels when expressed in bacteria

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2020
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Araya Flores, Jorge
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Solanum lycopersicum (tomato) possesses mitochondrial and plastidial lipoyl synthases capable of increasing lipoylation levels when expressed in bacteria
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  • Araya Flores, Jorge;
  • Miranda, Simon;
  • Covarrubias Becerra, María Paz;
  • Stange Klein, Claudia;
  • Handford, Michael;
Abstract
Lipoic 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.
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Comisión 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 Chile
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URI: https://repositorio.uchile.cl/handle/2250/175574
DOI: 10.1016/j.plaphy.2020.03.031
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Plant Physiol Biochem Volume: 151 Pages: 264-270 Jun 2020
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