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[PMID]:29355496
[Au] Autor:Lee S; Cheung-See-Kit M; Williams TA; Yamout N; Zufferey R
[Ad] Endereço:Department of Biological Sciences, St John's University, 8000 Utopia Parkway, Jamaica, NY 11439, USA.
[Ti] Título:The glycosomal alkyl-dihydroxyacetonephosphate synthase TbADS is essential for the synthesis of ether glycerophospholipids in procyclic trypanosomes.
[So] Source:Exp Parasitol;185:71-78, 2018 Feb.
[Is] ISSN:1090-2449
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glycerophospholipids are the main constituents of the biological membranes in Trypanosoma brucei, which causes sleeping sickness in humans. The present work reports the characterization of the alkyl-dihydroxyacetonephosphate synthase TbADS that catalyzes the committed step in ether glycerophospholipid biosynthesis. TbADS localizes to the glycosomal lumen. TbADS complemented a null mutant of Leishmania major lacking alkyl-dihydroxyacetonephosphate synthase activity and restored the formation of normal form of the ether lipid based virulence factor lipophosphoglycan. Despite lacking alkyl-dihydroxyacetonephosphate synthase activity, a null mutant of TbADS in procyclic trypanosomes remained viable and exhibited normal growth. Comprehensive analysis of cellular glycerophospholipids showed that TbADS was involved in the biosynthesis of all ether glycerophospholipid species, primarily found in the PE and PC classes.
[Mh] Termos MeSH primário: Alquil e Aril Transferases/metabolismo
Glicerofosfolipídeos/biossíntese
Leishmania major/enzimologia
Microcorpos/enzimologia
Trypanosoma brucei brucei/enzimologia
[Mh] Termos MeSH secundário: Leishmania major/genética
Leishmania major/metabolismo
Mutação com Perda de Função
Plasmídeos/química
Plasmídeos/genética
Plasmídeos/metabolismo
Espectrometria de Massas em Tandem
Trypanosoma brucei brucei/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycerophospholipids); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.26 (alkylglycerone-phosphate synthase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180123
[St] Status:MEDLINE


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[PMID]:28715456
[Au] Autor:Zufferey R; Pirani K; Cheung-See-Kit M; Lee S; Williams TA; Chen DG; Hossain MF
[Ad] Endereço:Department of Biochemistry, Kansas State University, Manhattan, Kansas, United States of America.
[Ti] Título:The Trypanosoma brucei dihydroxyacetonephosphate acyltransferase TbDAT is dispensable for normal growth but important for synthesis of ether glycerophospholipids.
[So] Source:PLoS One;12(7):e0181432, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glycerophospholipids are the most abundant constituents of biological membranes in Trypanosoma brucei, which causes sleeping sickness in humans and nagana in cattle. They are essential cellular components that fulfill various important functions beyond their structural role in biological membranes such as in signal transduction, regulation of membrane trafficking or control of cell cycle progression. Our previous studies have established that the glycerol-3-phosphate acyltransferase TbGAT is dispensable for growth, viability, and ester lipid biosynthesis suggesting the existence of another initial acyltransferase(s). This work presents the characterization of the alternative, dihydroxyacetonephosphate acyltransferase TbDAT, which acylates primarily dihydroxyacetonephosphate and prefers palmitoyl-CoA as an acyl-CoA donor. TbDAT restores the viability of a yeast double null mutant that lacks glycerol-3-phosphate and dihydroxyacetonephosphate acyltransferase activities. A conditional null mutant of TbDAT in T. brucei procyclic form was created and characterized. TbDAT was important for survival during stationary phase and synthesis of ether lipids. In contrast, TbDAT was dispensable for normal growth. Our results show that in T. brucei procyclic forms i) TbDAT but not TbGAT is the physiologically relevant initial acyltransferase and ii) ether lipid precursors are primarily made by TbDAT.
[Mh] Termos MeSH primário: Aciltransferases/metabolismo
Éteres Fosfolipídicos/metabolismo
Trypanosoma brucei brucei/enzimologia
Trypanosoma brucei brucei/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Aciltransferases/genética
Western Blotting
Eletroforese em Gel de Poliacrilamida
Imunofluorescência
Microcorpos/metabolismo
Mutação
Espectrometria de Massas por Ionização por Electrospray
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phospholipid Ethers); EC 2.3.- (Acyltransferases); EC 2.3.1.42 (glycerone-phosphate O-acyltransferase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181432


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[PMID]:28426655
[Au] Autor:Bauer S; Morris MT
[Ad] Endereço:Eukaryotic Pathogens Innovation Center, Department of Genetics and Biochemistry, Clemson University, Clemson, South Carolina, United States of America.
[Ti] Título:Glycosome biogenesis in trypanosomes and the de novo dilemma.
[So] Source:PLoS Negl Trop Dis;11(4):e0005333, 2017 Apr.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Trypanosomatid parasites, including Trypanosoma and Leishmania, are the causative agents of lethal diseases threatening millions of people around the world. These organisms compartmentalize glycolysis in essential, specialized peroxisomes called glycosomes. Peroxisome proliferation can occur through growth and division of existing organelles and de novo biogenesis from the endoplasmic reticulum. The level that each pathway contributes is debated. Current evidence supports the concerted contribution of both mechanisms in an equilibrium that can vary depending on environmental conditions and metabolic requirements of the cell. Homologs of a number of peroxins, the proteins involved in peroxisome biogenesis and matrix protein import, have been identified in T. brucei. Based on these findings, it is widely accepted that glycosomes proliferate through growth and division of existing organelles; however, to our knowledge, a de novo mechanism of biogenesis has not been directly demonstrated. Here, we review recent findings that provide support for the existence of an endoplasmic reticulum (ER)-derived de novo pathway of glycosome biogenesis in T. brucei. Two studies recently identified PEX13.1, a peroxin involved in matrix protein import, in the ER of procyclic form T. brucei. In other eukaryotes, peroxins including PEX13 have been found in the ER of cells undergoing de novo biogenesis of peroxisomes. In addition, PEX16 and PEX19 have been characterized in T. brucei, both of which are important for de novo biogenesis in other eukaryotes. Because glycosomes are rapidly remodeled via autophagy during life cycle differentiation, de novo biogenesis could provide a method of restoring glycosome populations following turnover. Together, the findings we summarize provide support for the hypothesis that glycosome proliferation occurs through growth and division of pre-existing organelles and de novo biogenesis of new organelles from the ER and that the level each mechanism contributes is influenced by glucose availability.
[Mh] Termos MeSH primário: Leishmania/crescimento & desenvolvimento
Proteínas de Membrana/metabolismo
Microcorpos/metabolismo
Peroxissomos/metabolismo
Proteínas de Protozoários/metabolismo
Trypanosoma brucei brucei/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Autofagia
Diferenciação Celular
Retículo Endoplasmático
Estágios do Ciclo de Vida
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (Protozoan Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170830
[Lr] Data última revisão:
170830
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170421
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0005333


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[PMID]:28360328
[Au] Autor:Dawidowski M; Emmanouilidis L; Kalel VC; Tripsianes K; Schorpp K; Hadian K; Kaiser M; Mäser P; Kolonko M; Tanghe S; Rodriguez A; Schliebs W; Erdmann R; Sattler M; Popowicz GM
[Ad] Endereço:Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany.
[Ti] Título:Inhibitors of PEX14 disrupt protein import into glycosomes and kill parasites.
[So] Source:Science;355(6332):1416-1420, 2017 03 31.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The parasitic protists of the genus infect humans and domestic mammals, causing severe mortality and huge economic losses. The most threatening trypanosomiasis is Chagas disease, affecting up to 12 million people in the Americas. We report a way to selectively kill by blocking glycosomal/peroxisomal import that depends on the PEX14-PEX5 protein-protein interaction. We developed small molecules that efficiently disrupt the PEX14-PEX5 interaction. This results in mislocalization of glycosomal enzymes, causing metabolic catastrophe, and it kills the parasite. High-resolution x-ray structures and nuclear magnetic resonance data enabled the efficient design of inhibitors with trypanocidal activities comparable to approved medications. These results identify PEX14 as an "Achilles' heel" of the suitable for the development of new therapies against trypanosomiases and provide the structural basis for their development.
[Mh] Termos MeSH primário: Proteínas de Membrana/antagonistas & inibidores
Proteínas de Protozoários/antagonistas & inibidores
Bibliotecas de Moléculas Pequenas/farmacologia
Tripanossomicidas/farmacologia
Trypanosoma brucei brucei/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Doença de Chagas/tratamento farmacológico
Desenho de Drogas
Seres Humanos
Proteínas de Membrana/química
Microcorpos/efeitos dos fármacos
Microcorpos/metabolismo
Ressonância Magnética Nuclear Biomolecular
Receptor 1 de Sinal de Orientação para Peroxissomos
Peroxissomos/efeitos dos fármacos
Peroxissomos/metabolismo
Domínios Proteicos
Transporte Proteico/efeitos dos fármacos
Proteínas de Protozoários/química
Receptores Citoplasmáticos e Nucleares/antagonistas & inibidores
Receptores Citoplasmáticos e Nucleares/química
Receptores Citoplasmáticos e Nucleares/metabolismo
Bibliotecas de Moléculas Pequenas/química
Bibliotecas de Moléculas Pequenas/uso terapêutico
Tripanossomicidas/química
Tripanossomicidas/uso terapêutico
Tripanossomíase Africana/tratamento farmacológico
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (PEX14 protein, Trypanosoma brucei); 0 (PEX5 protein, human); 0 (Peroxisome-Targeting Signal 1 Receptor); 0 (Protozoan Proteins); 0 (Receptors, Cytoplasmic and Nuclear); 0 (Small Molecule Libraries); 0 (Trypanocidal Agents)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170401
[St] Status:MEDLINE
[do] DOI:10.1126/science.aal1807


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[PMID]:28348078
[Au] Autor:Lin S; Voyton C; Morris MT; Ackroyd PC; Morris JC; Christensen KA
[Ad] Endereço:From the Departments of Chemistry and.
[Ti] Título:pH regulation in glycosomes of procyclic form .
[So] Source:J Biol Chem;292(19):7795-7805, 2017 May 12.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Here we report the use of a fluorescein-tagged peroxisomal targeting sequence peptide (F-PTS1, acetyl-C{K(FITC)}GGAKL) for investigating pH regulation of glycosomes in live procyclic form When added to cells, this fluorescent peptide is internalized within vesicular structures, including glycosomes, and can be visualized after 30-60 min. Using F-PTS1 we are able to observe the pH conditions inside glycosomes in response to starvation conditions. Previous studies have shown that in the absence of glucose, the glycosome exhibits mild acidification from pH 7.4 ± 0.2 to 6.8 ± 0.2. Our results suggest that this response occurs under proline starvation as well. This pH regulation is found to be independent from cytosolic pH and requires a source of Na ions. Glycosomes were also observed to be more resistant to external pH changes than the cytosol; placement of cells in acidic buffers (pH 5) reduced the pH of the cytosol by 0.8 ± 0.1 pH units, whereas glycosomal pH decreases by 0.5 ± 0.1 pH units. This observation suggests that regulation of glycosomal pH is different and independent from cytosolic pH regulation. Furthermore, pH regulation is likely to work by an active process, because cells depleted of ATP with 2-deoxyglucose and sodium azide were unable to properly regulate pH. Finally, inhibitor studies with bafilomycin and EIPA suggest that both V-ATPases and Na /H exchangers are required for glycosomal pH regulation.
[Mh] Termos MeSH primário: Microcorpos/química
Trypanosoma brucei brucei/química
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/química
Amilorida/análogos & derivados
Amilorida/química
Animais
Citosol/química
Desoxiglucose/química
Digitonina/química
Glucose/química
Homeostase
Concentração de Íons de Hidrogênio
Macrolídeos/química
Microscopia de Fluorescência
Potássio/química
Prolina/química
Domínios Proteicos
Proteínas de Protozoários/química
Azida Sódica/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Macrolides); 0 (Protozoan Proteins); 116764-51-3 (bafilomycin A); 7DZO8EB0Z3 (Amiloride); 8L70Q75FXE (Adenosine Triphosphate); 968JJ8C9DV (Sodium Azide); 9DLQ4CIU6V (Proline); 9G2MP84A8W (Deoxyglucose); IY9XDZ35W2 (Glucose); KOO5CM684H (Digitonin); RWP5GA015D (Potassium); VW50CE070T (ethylisopropylamiloride)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170329
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.784173


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[PMID]:27795357
[Au] Autor:Boitz JM; Gilroy CA; Olenyik TD; Paradis D; Perdeh J; Dearman K; Davis MJ; Yates PA; Li Y; Riscoe MK; Ullman B; Roberts SC
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Oregon Health & Science University, Portland, Oregon, USA.
[Ti] Título:Arginase Is Essential for Survival of Leishmania donovani Promastigotes but Not Intracellular Amastigotes.
[So] Source:Infect Immun;85(1), 2017 Jan.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Studies of Leishmania donovani have shown that both ornithine decarboxylase and spermidine synthase, two enzymes of the polyamine biosynthetic pathway, are critical for promastigote proliferation and required for maximum infection in mice. However, the importance of arginase (ARG), the first enzyme of the polyamine pathway in Leishmania, has not been analyzed in L. donovani To test ARG function in intact parasites, we generated Δarg null mutants in L. donovani and evaluated their ability to proliferate in vitro and trigger infections in mice. The Δarg knockout was incapable of growth in the absence of polyamine supplementation, but the auxotrophic phenotype could be bypassed by addition of either millimolar concentrations of ornithine or micromolar concentrations of putrescine or by complementation with either glycosomal or cytosolic versions of ARG. Spermidine supplementation of the medium did not circumvent the polyamine auxotrophy of the Δarg line. Although ARG was found to be essential for ornithine and polyamine synthesis, ornithine decarboxylase appeared to be the rate-limiting enzyme for polyamine production. Mouse infectivity studies revealed that the Δarg lesion reduced parasite burdens in livers by an order of magnitude but had little impact on the numbers of parasites recovered from spleens. Thus, ARG is essential for proliferation of promastigotes but not intracellular amastigotes. Coupled with previous studies, these data support a model in which L. donovani amastigotes readily salvage ornithine and have some access to host spermidine pools, while host putrescine appears to be unavailable for salvage by the parasite.
[Mh] Termos MeSH primário: Arginase/metabolismo
Leishmania donovani/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Citosol/metabolismo
Citosol/parasitologia
Feminino
Leishmania infantum/metabolismo
Leishmania infantum/parasitologia
Leishmaniose Visceral/metabolismo
Leishmaniose Visceral/parasitologia
Camundongos
Camundongos Endogâmicos BALB C
Microcorpos/metabolismo
Microcorpos/parasitologia
Ornitina Descarboxilase/metabolismo
Poliaminas/metabolismo
Putrescina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polyamines); EC 3.5.3.1 (Arginase); EC 4.1.1.17 (Ornithine Decarboxylase); V10TVZ52E4 (Putrescine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170516
[Lr] Data última revisão:
170516
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161101
[St] Status:MEDLINE


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[PMID]:27339640
[Au] Autor:Bauer ST; McQueeney KE; Patel T; Morris MT
[Ad] Endereço:Department of Genetics and Biochemistry, Eukaryotic Pathogens Innovation Center, Clemson University, Clemson, South Carolina, 29634.
[Ti] Título:Localization of a Trypanosome Peroxin to the Endoplasmic Reticulum.
[So] Source:J Eukaryot Microbiol;64(1):97-105, 2017 Jan.
[Is] ISSN:1550-7408
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Trypanosoma brucei is the causative agent of diseases that affect 30,000-50,000 people annually. Trypanosoma brucei harbors unique organelles named glycosomes that are essential to parasite survival, which requires growth under fluctuating environmental conditions. The mechanisms that govern the biogenesis of these organelles are poorly understood. Glycosomes are evolutionarily related to peroxisomes, which can proliferate de novo from the endoplasmic reticulum or through the growth and division of existing organelles depending on the organism and environmental conditions. The effect of environment on glycosome biogenesis is unknown. Here, we demonstrate that the glycosome membrane protein, TbPex13.1, is localized to glycosomes when cells are cultured under high glucose conditions and to the endoplasmic reticulum in low glucose conditions. This localization in low glucose was dependent on the presence of a C-terminal tripeptide sequence. Our findings suggest that glycosome biogenesis is influenced by extracellular glucose levels and adds to the growing body of evidence that de novo glycosome biogenesis occurs in trypanosomes. Because the movement of peroxisomal membrane proteins is a hallmark of ER-dependent peroxisome biogenesis, TbPex13.1 may be a useful marker for the study such processes in trypanosomes.
[Mh] Termos MeSH primário: Retículo Endoplasmático/metabolismo
Proteínas de Membrana/metabolismo
Microcorpos/metabolismo
Proteínas de Protozoários/metabolismo
Trypanosoma brucei brucei/metabolismo
[Mh] Termos MeSH secundário: Glucose/administração & dosagem
Glucose/metabolismo
Proteínas de Membrana/genética
Peroxissomos/genética
Peroxissomos/metabolismo
Proteínas de Protozoários/genética
Trypanosoma brucei brucei/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (Protozoan Proteins); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160625
[St] Status:MEDLINE
[do] DOI:10.1111/jeu.12343


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[PMID]:27312997
[Au] Autor:Lobo-Rojas ÁE; González-Marcano EB; Valera-Vera EA; Acosta HR; Quiñones WA; Burchmore RJ; Concepción JL; Cáceres AJ
[Ad] Endereço:Laboratorio de Enzimología de Parásitos, Facultad de Ciencias, Universidad de Los Andes, La Hechicera, 5101 Mérida, Venezuela.
[Ti] Título:Trypanosoma cruzi contains two galactokinases; molecular and biochemical characterization.
[So] Source:Parasitol Int;65(5 Pt A):472-82, 2016 Oct.
[Is] ISSN:1873-0329
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Two different putative galactokinase genes, found in the genome database of Trypanosoma cruzi were cloned and sequenced. Expression of the genes in Escherichia coli resulted for TcGALK-1 in the synthesis of a soluble and active enzyme, and in the case of TcGALK-2 gene a less soluble protein, with predicted molecular masses of 51.9kDa and 51.3kDa, respectively. The Km values determined for the recombinant proteins were for galactose 0.108mM (TcGALK-1) and 0.091mM (TcGALK-2) and for ATP 0.36mM (TcGALK-1) and 0.1mM (TcGALK-2). Substrate inhibition by ATP (Ki 0.414mM) was only observed for TcGALK-2. Gel-filtration chromatography showed that natural TcGALKs and recombinant TcGALK-1 are monomeric. In agreement with the possession of a type-1 peroxisome-targeting signal by both TcGALKs, they were found to be present inside glycosomes using two different methods of subcellular fractionation in conjunction with mass spectrometry. Both genes are expressed in epimastigote and trypomastigote stages since the respective proteins were immunodetected by western blotting. The T. cruzi galactokinases present their highest (52-47%) sequence identity with their counterpart from Leishmania spp., followed by prokaryotic galactokinases such as those from E. coli and Lactococcus lactis (26-23%). In a phylogenetic analysis, the trypanosomatid galactokinases form a separate cluster, showing an affiliation with bacteria. Epimastigotes of T. cruzi can grow in glucose-depleted LIT-medium supplemented with 20mM of galactose, suggesting that this hexose, upon phosphorylation by a TcGALK, could be used in the synthesis of UDP-galactose and also as a possible carbon and energy source.
[Mh] Termos MeSH primário: Galactoquinase/genética
Galactose/metabolismo
Proteínas Recombinantes/genética
Trypanosoma cruzi/genética
Trypanosoma cruzi/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sequência de Bases
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Microcorpos/metabolismo
Análise de Sequência de DNA
Trypanosoma cruzi/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); EC 2.7.1.6 (Galactokinase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170313
[Lr] Data última revisão:
170313
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160618
[St] Status:MEDLINE


  9 / 4530 MEDLINE  
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[PMID]:27170716
[Au] Autor:Morales J; Hashimoto M; Williams TA; Hirawake-Mogi H; Makiuchi T; Tsubouchi A; Kaga N; Taka H; Fujimura T; Koike M; Mita T; Bringaud F; Concepción JL; Hashimoto T; Embley TM; Nara T
[Ad] Endereço:Department of Molecular and Cellular Parasitology, Juntendo University Graduate School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113-8421, Japan.
[Ti] Título:Differential remodelling of peroxisome function underpins the environmental and metabolic adaptability of diplonemids and kinetoplastids.
[So] Source:Proc Biol Sci;283(1830), 2016 05 11.
[Is] ISSN:1471-2954
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The 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.
[Mh] Termos MeSH primário: Euglenozoários/citologia
Euglenozoários/metabolismo
Peroxissomos/metabolismo
Trypanosoma cruzi/citologia
[Mh] Termos MeSH secundário: Aminoácidos/metabolismo
Carbono/metabolismo
Enzimas/metabolismo
Euglenozoários/genética
Gluconeogênese
Microcorpos
Via de Pentose Fosfato
Filogenia
Transdução de Sinais
Trypanosoma cruzi/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids); 0 (Enzymes); 7440-44-0 (Carbon)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160513
[St] Status:MEDLINE


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[PMID]:27021571
[Au] Autor:Borst P
[Ad] Endereço:The Netherlands Cancer Institute, Plesmanlaan 121, 1066CX Amsterdam, The Netherlands. Electronic address: p.borst@nki.nl.
[Ti] Título:Maxi-circles, glycosomes, gene transposition, expression sites, transsplicing, transferrin receptors and base J.
[So] Source:Mol Biochem Parasitol;205(1-2):39-52, 2016 Jan-Feb.
[Is] ISSN:1872-9428
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:This is a personal story of the author of his research on trypanosomatids, covering a period of 1970-2015. Some of the highlights include the discovery of new aspects of kDNA, the mini-circle heterogeneity and the maxi-circle; the glycosome; the discovery of gene transposition as a major mechanism for antigenic variation; trans-splicing as an essential step in the synthesis of all trypanosome mRNAs; Pulsed Field Gradient gels to size-fractionate chromosome-sized DNA molecules of protozoa; the sequence of trypanosome telomeres and their growth and contraction; the first ABC-transporter of trypanosomatids, LtpgpA; the variable transferrin receptor of T. brucei and its role in Fe uptake; and base J, its structure, biosynthesis and function.
[Mh] Termos MeSH primário: Kinetoplastida/genética
Kinetoplastida/metabolismo
Microcorpos/química
Parasitologia/história
[Mh] Termos MeSH secundário: Bélgica
DNA de Cinetoplasto
Expressão Gênica
Genômica
História do Século XX
Kinetoplastida/química
Kinetoplastida/citologia
[Pt] Tipo de publicação:AUTOBIOGRAPHY; HISTORICAL ARTICLE; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Ps] Nome de pessoa como assunto:Borst P
[Nm] Nome de substância:
0 (DNA, Kinetoplast)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160330
[St] Status:MEDLINE



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