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Differential remodelling of peroxisome function underpins the environmental and metabolic adaptability of diplonemids and kinetoplastids.

dc.rights.licenseopenen_US
dc.contributor.authorMORALES, Jorge
dc.contributor.authorHASHIMOTO, Muneaki
dc.contributor.authorWILLIAMS, Tom A
dc.contributor.authorHIRAWAKE-MOGI, Hiroko
dc.contributor.authorMAKIUCHI, Takashi
dc.contributor.authorTSUBOUCHI, Akiko
dc.contributor.authorKAGA, Naoko
dc.contributor.authorTAKA, Hikari
dc.contributor.authorFUJIMURA, Tsutomu
dc.contributor.authorKOIKE, Masato
dc.contributor.authorMITA, Toshihiro
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorBRINGAUD, Frederic
dc.contributor.authorCONCEPCIÓN, Juan L
dc.contributor.authorHASHIMOTO, Tetsuo
dc.contributor.authorEMBLEY, T Martin
dc.contributor.authorNARA, Takeshi
dc.date.accessioned2023-11-03T09:40:57Z
dc.date.available2023-11-03T09:40:57Z
dc.date.issued2016-05-11
dc.identifier.issn1471-2954en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/184583
dc.description.abstractEnThe remodelling of organelle function is increasingly appreciated as a central driver of eukaryotic biodiversity and evolution. Kinetoplastids including Trypanosoma and Leishmania have evolved specialized peroxisomes, called glycosomes. Glycosomes uniquely contain a glycolytic pathway as well as other enzymes, which underpin the physiological flexibility of these major human pathogens. The sister group of kinetoplastids are the diplonemids, which are among the most abundant eukaryotes in marine plankton. Here we demonstrate the compartmentalization of gluconeogenesis, or glycolysis in reverse, in the peroxisomes of the free-living marine diplonemid, Diplonema papillatum Our results suggest that peroxisome modification was already under way in the common ancestor of kinetoplastids and diplonemids, and raise the possibility that the central importance of gluconeogenesis to carbon metabolism in the heterotrophic free-living ancestor may have been an important selective driver. Our data indicate that peroxisome modification is not confined to the kinetoplastid lineage, but has also been a factor in the success of their free-living euglenozoan relatives.
dc.language.isoENen_US
dc.subject.enAmino Acids
dc.subject.enCarbon
dc.subject.enEnzymes
dc.subject.enEuglenozoa
dc.subject.enGluconeogenesis
dc.subject.enMicrobodies
dc.subject.enPentose Phosphate Pathway
dc.subject.enPeroxisomes
dc.subject.enPhylogeny
dc.subject.enSignal Transduction
dc.subject.enTrypanosoma cruzi
dc.title.enDifferential remodelling of peroxisome function underpins the environmental and metabolic adaptability of diplonemids and kinetoplastids.
dc.title.alternativeProc Biol Scien_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1098/rspb.2016.0520en_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologieen_US
dc.identifier.pubmed27170716en_US
bordeaux.journalProceedings of the Royal Society B: Biological Sciencesen_US
bordeaux.volume283en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.issue1830en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcepubmed
hal.identifierhal-04269240
hal.version1
hal.date.transferred2023-11-03T09:41:01Z
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exporttrue
workflow.import.sourcepubmed
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Proceedings%20of%20the%20Royal%20Society%20B:%20Biological%20Sciences&rft.date=2016-05-11&rft.volume=283&rft.issue=1830&rft.eissn=1471-2954&rft.issn=1471-2954&rft.au=MORALES,%20Jorge&HASHIMOTO,%20Muneaki&WILLIAMS,%20Tom%20A&HIRAWAKE-MOGI,%20Hiroko&MAKIUCHI,%20Takashi&rft.genre=article


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