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The SCP2-thiolase-like protein (SLP) of Trypanosoma brucei is an enzyme involved in lipid metabolism

dc.rights.licenseopenen_US
dc.contributor.authorHARIJAN, Rajesh K.
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorMAZET, Muriel
dc.contributor.authorKIEMA, Tiila R.
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorBOUYSSOU, Guillaume
dc.contributor.authorALEXSON, Stefan E. H.
dc.contributor.authorBERGMANN, Ulrich
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorMOREAU, Patrick
IDREF: 058610723
dc.contributor.authorMICHELS, Paul A. M.
hal.structure.identifierCentre de résonance magnétique des systèmes biologiques [CRMSB]
dc.contributor.authorBRINGAUD, Frederic
dc.contributor.authorWIERENGA, Rik K.
dc.date.accessioned2023-07-06T07:33:32Z
dc.date.available2023-07-06T07:33:32Z
dc.date.issued2016
dc.identifier.issn0887-3585en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/183315
dc.description.abstractEnBioinformatics studies have shown that the genomes of trypanosomatid species each encode one SCP2-thiolase-like protein (SLP), which is characterized by having the YDCF thiolase sequence fingerprint of the C beta 2-C alpha 2 loop. SLPs are only encoded by the genomes of these parasitic protists and not by those of mammals, including human. Deletion of the Trypanosoma brucei SLP gene (TbSLP) increases the doubling time of procyclic T. brucei and causes a 5-fold reduction of de novo sterol biosynthesis from glucose-and acetate-derived acetyl-CoA. Fluorescence analyses of EGFP-tagged TbSLP expressed in the parasite located the TbSLP in the mitochondrion. The crystal structure of TbSLP (refined at 1.75 angstrom resolution) confirms that TbSLP has the canonical dimeric thiolase fold. In addition, the structures of the TbSLP-acetoacetyl-CoA (1.90 angstrom) and TbSLP-malonyl-CoA (2.30 angstrom) complexes reveal that the two oxyanion holes of the thiolase active site are preserved. TbSLP binds malonyl-CoA tightly (K-d 90 mu M), acetoacetyl-CoA moderately (K-d 0.9 mM) and acetyl-CoA and CoA very weakly. TbSLP possesses low malonyl-CoA decarboxylase activity. Altogether, the data show that TbSLP is a mitochondrial enzyme involved in lipid metabolism.
dc.language.isoENen_US
dc.subject.encrystal structure
dc.subject.enmitochondrial lipid metabolism
dc.subject.engene knockout
dc.subject.enmalonyl-CoA:ACP transacylase
dc.subject.enmalonyl-CoA decarboxylase
dc.subject.enSCP2-thiolase-like protein
dc.subject.enSCP2-thiolase
dc.subject.enTrypanosoma brucei
dc.title.enThe SCP2-thiolase-like protein (SLP) of Trypanosoma brucei is an enzyme involved in lipid metabolism
dc.typeArticle de revueen_US
dc.identifier.doi10.1002/prot.25054en_US
dc.subject.halSciences du Vivant [q-bio]en_US
bordeaux.page1075-1096en_US
bordeaux.volume84en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.issue8en_US
bordeaux.institutionCNRSen_US
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionINRAE
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcehal
hal.identifierhal-01602832
hal.version1
hal.popularnonen_US
hal.audienceNon spécifiéeen_US
hal.exportfalse
workflow.import.sourcehal
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