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dc.contributor.authorGuenther, Svenja
dc.contributor.authorWallace, Lynsey
dc.contributor.authorPatzewitz, Eva-Maria
dc.contributor.authorMcMillan, Paul J.
dc.contributor.authorStorm, Janet
dc.contributor.authorWrenger, Carsten
dc.contributor.authorBissett, Ryan
dc.contributor.authorSmith, Terry K
dc.contributor.authorMueller, Sylke
dc.date.accessioned2013-12-03T10:01:05Z
dc.date.available2013-12-03T10:01:05Z
dc.date.issued2007-12
dc.identifier.citationGuenther , S , Wallace , L , Patzewitz , E-M , McMillan , P J , Storm , J , Wrenger , C , Bissett , R , Smith , T K & Mueller , S 2007 , ' Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum ' , PLoS Pathogens , vol. 3 , no. 12 , e189 , pp. 1938-1949 . https://doi.org/10.1371/journal.ppat.0030189en
dc.identifier.issn1553-7366
dc.identifier.otherPURE: 3439331
dc.identifier.otherPURE UUID: 3c098021-2137-4760-a8a8-a1557cfcb71a
dc.identifier.otherWOS: 000253296400011
dc.identifier.otherScopus: 37849040526
dc.identifier.urihttp://hdl.handle.net/10023/4242
dc.description.abstractLipoic acid (LA) is an essential cofactor of alpha-keto acid dehydrogenase complexes (KADHs) and the glycine cleavage system. In Plasmodium, LA is attached to the KADHs by organelle-specific lipoylation pathways. Biosynthesis of LA exclusively occurs in the apicoplast, comprising octanoyl-[acyl carrier protein]: protein N-octanoyltransferase (LipB) and LA synthase. Salvage of LA is mitochondrial and scavenged LA is ligated to the KADHs by LA protein ligase 1 (LplA1). Both pathways are entirely independent, suggesting that both are likely to be essential for parasite survival. However, disruption of the LipB gene did not negatively affect parasite growth despite a drastic loss of LA (> 90%). Surprisingly, the sole, apicoplast-located pyruvate dehydrogenase still showed lipoylation, suggesting that an alternative lipoylation pathway exists in this organelle. We provide evidence that this residual lipoylation is attributable to the dual targeted, functional lipoate protein ligase 2 (LplA2). Localisation studies show that LplA2 is present in both mitochondrion and apicoplast suggesting redundancy between the lipoic acid protein ligases in the erythrocytic stages of P. falciparum.
dc.format.extent12
dc.language.isoeng
dc.relation.ispartofPLoS Pathogensen
dc.rights© 2007 Günther et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en
dc.subjectESCHERICHIA-COLIen
dc.subjectAPICOMPLEXAN PARASITESen
dc.subjectLIPOYLATION PATHWAYSen
dc.subjectARABIDOPSIS-THALIANAen
dc.subjectTOXOPLASMA-GONDIIen
dc.subjectMALARIA PARASITESen
dc.subjectCRYSTAL-STRUCTUREen
dc.subjectBOVINE LIVERen
dc.subjectLIPB GENESen
dc.subjectLIPOATEen
dc.titleApicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparumen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.identifier.doihttps://doi.org/10.1371/journal.ppat.0030189
dc.description.statusPeer revieweden
dc.identifier.urlhttp://www.scopus.com/inward/record.url?scp=37849040526&partnerID=8YFLogxKen


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