Transketolase in Trypanosoma brucei

التفاصيل البيبلوغرافية
العنوان: Transketolase in Trypanosoma brucei
المؤلفون: Vincent P. Alibu, Michael P. Barrett, Jean-Charles Portais, Frédéric Bringaud, Jane Hubert, Sabine A. Stoffel, Charles Ebikeme, M. Ernst Schweingruber
المساهمون: Pev Biotech AG, Partenaires INRAE, University of Glasgow, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Université de Bordeaux Ségalen [Bordeaux 2], Universität Bern- University of Bern [Bern], Swiss National Foundation, Wellcome Trust, Agence Nationale de la Recherche (ANR) [ANR-MIME2007], BBSRC-ANR, Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)
المصدر: Molecular and Biochemical Parasitology
Molecular and Biochemical Parasitology, Elsevier, 2011, 179 (1), pp.1-7. ⟨10.1016/j.molbiopara.2011.04.006⟩
Molecular and Biochemical Parasitology, 2011, 179 (1), pp.1-7. ⟨10.1016/j.molbiopara.2011.04.006⟩
بيانات النشر: HAL CCSD, 2011.
سنة النشر: 2011
مصطلحات موضوعية: [SDV]Life Sciences [q-bio], Trypanosoma brucei brucei, Mutant, Gene Expression, Protein Sorting Signals, Transketolase, Biology, Trypanosoma brucei, METABOLISM, Microbodies, 03 medical and health sciences, chemistry.chemical_compound, Cytosol, [SDV.IDA]Life Sciences [q-bio]/Food engineering, Escherichia coli, Metabolic profiling, BLOOD-STREAM FORMS, [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering, OXIDATIVE STRESS, PENTOSE-PHOSPHATE PATHWAY, LEISHMANIA-MEXICANA, Molecular Biology, Gene, Peroxisomal targeting signal, Pentose phosphate pathway, 030304 developmental biology, Pentosephosphates, 0303 health sciences, THIAMIN CATALYSIS, Gene Expression Profiling, 030302 biochemistry & molecular biology, Wild type, biology.organism_classification, Molecular biology, Recombinant Proteins, LIFE-CYCLE STAGES, Kinetics, Protein Transport, Sedoheptulose, chemistry, Biochemistry, ESCHERICHIA-COLI, Ttypanosoma brucei, Transketolase activity, Parasitology, Ribosemonophosphates, DIPHOSPHATE-DEPENDENT ENZYME, MESSENGER-RNA
الوصف: International audience; A single copy gene, encoding a protein highly similar to transketolase from other systems, was identified in the Trypanosoma brucei genome. The gene was expressed in E. coil and the purified protein demonstrated transketolase activity with Km values of 0.2 mM and 0.8 mM respectively for xylulose 5-phosphate and ribose 5-phosphate. A peroxisomal targeting signal (PTS-1) present at the C-terminus of the protein suggested a glycosomal localisation. However, subcellular localisation experiments revealed that while the protein was present in glycosomes it was found mainly within the cytosol and thus has a dual localisation. Transketolase activity was absent from the long slender bloodstream form of the parasite and the protein was not detectable in this life cycle stage, with the RNA present only at low abundance, indicating a strong differential regulation, being present predominantly in the procyclic form. The gene was knocked out from procyclic T. brucei and transketolase activity was lost but no growth phenotype was evident in the null mutants. Metabolite profiling to compare wild type and TKT null mutants revealed substantial increases in transketolase substrate metabolites coupled to loss of sedoheptulose 7-phosphate, a principal product of the transketolase reaction. (C) 2011 Elsevier B.V. All rights reserved.
اللغة: English
تدمد: 0166-6851
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed9cef70bc8cc0854379e83db76f6993
https://hal.inrae.fr/hal-02644262
حقوق: CLOSED
رقم الأكسشن: edsair.doi.dedup.....ed9cef70bc8cc0854379e83db76f6993
قاعدة البيانات: OpenAIRE