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| Chevrollier, A.; Loiseau, D.; Chabi, B.; Renier, G.; Douay, O.; Malthièry, Y.; Stepien, G.. |
| The three adenine nucleotide translocator (ANT1 to ANT3) isoforms, differentially expressed in human cells, play a crucial role in cell bioenergetics by catalyzing ADP and ATP exchange across the mitochondrial inner membrane. In contrast to differentiated tissue cells, transformed cells, and their rho(0) derivatives, i.e. cells deprived of mitochondrial DNA, sustain a high rate of glycolysis. We compared the expression pattern of ANT isoforms in several transformed human cell lines at different stages of the cell cycle. The level of ANT2 expression and glycolytic ATP production in these cell lines were in keeping with their metabolic background and their state of differentiation. The sensitivity of the mitochondrial inner membrane potential (Delta psi) to... |
| Tipo: Journal Article |
Palavras-chave: CARCINOGENESE; ADENINE NUCLEOTIDE TRANSLOCATOR CARCINOGENESIS; MITOCHONDRIA; GLYCOLYSIS; ADENINE NUCLEOTIDE TRANSLOCATOR. |
| Ano: 2005 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2009b292a44&uri=/notices/prodinra1/2010/11/ |
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| Smiri, M.; Chaoui, A.; Rouhier, N.; Chibani, K.; Gelhaye, É.; Jacquot, J.P.; El Ferjani, E. |
| Mitochondria play an essential role in producing the energy required for seedling growth following imbibition. Heavy metals, such as cadmium impair mitochondrial functioning in part by altering redox regulation. The activities of two protein redox systems present in mitochondria, thioredoxin (Trx) and glutaredoxin (Grx), were analysed in the cotyledons and embryo of pea (Pisum sativum L.) germinating seeds exposed to toxic Cd concentration. Compared to controls, Cd-treated germinating seeds showed a decrease in total soluble protein content, but an increase in –SH content. Under Cd stress conditions, Grx and glutathione reductase (GR) activities as well as glutathione (GSH) concentrations decreased both in cotyledons and the embryo. Similar results were... |
| Tipo: Journal Article |
Palavras-chave: PEA; COTYLEDONS; EMBRYO; HEAVY METALS; CADMIUM; GERMINATING SEEDS; MITOCHONDRIA; REDOX; THIOREDOXIN; GLUTAREDOXIN; GLUTATHIONE REDUCTASE; NADPH-DEPENDENT THIOREDOXIN REDUCTASE; NAD(P)H OXIDASE; OXIDATIVE STRESS. |
| Ano: 2010 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD201014da3708&uri=/notices/prodinra1/2010/11/ |
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| Peeters, N.M.; Chapron, A.; Giritch, A.; Grandjean, O.; Lancelin, D.; Lhomme, T.; Vivrel, A.; Small, I.. |
| Two cysteinyl-tRNA synthetases (CysRS) and four asparaginyl-tRNA synthetases (AsnRS) from Arabidopsis thaliana were characterized from genome sequence data, EST sequences, and RACE sequences. For one CysRS and one AsnRS, sequence alignments and prediction programs suggested the presence of an N-terminal organellar targeting peptide. Transient expression of these putative targeting sequences joined to jellyfish green fluorescent protein (GFP) demonstrated that both presequences can efficiently dual-target GFP to mitochondria and plastids. The other CysRS and AsnRSs lack targeting sequences and presumably aminoacylate cytosolic tRNAs. Phylogenetic analysis suggests that the four AsnRSs evolved by repeated duplication of a gene transferred from an ancestral... |
| Tipo: Journal Article |
Palavras-chave: AMINOACYL-ARNT SYNTHETASE; PLASTIDE; DUPLICATION DE GENE; ARABIDOPSIS THALIANA; PLANTE; ORGANITE; DOUBLE CIBLAGE; GFP; EST AMINOACYL-tRNA SYNTHETASE; MITOCHONDRIA; PLASTIDS; GENE DUPLICATION; DUAL-TARGETING. |
| Ano: 2000 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0100023509086627&uri=/notices/prodinra1/2010/11/ |
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| Barroso, G.; Sirand-Pugnet, P.; Mouhamadou, B.; Labarère, J.. |
| The complete sequences and secondary structures of the mitochondrial small subunit (SSU) ribosomal RNAs of both mostly cultivated mushrooms Agaricus bisporus (1930 nt) and Lentinula edodes (2164 nt) were achieved. These secondary structures and that of Schizophyllum commune (1872 nt) were compared to that previously established for Agrocybe aegerita. The four structures are near the model established for Archae, Bacteria, plastids, and mitochondria; particularly the helices 23 and 37, described as specific to bacteria, are present. Within the four Agaricales (Homobasidiomycota), the SSU-rRNA ldquocorerdquo is conserved in size (966 to 1009 nt) with the exception of an unusual extension of 40 nt in the H17 helix of S. commune. The four core sequences... |
| Tipo: Journal Article |
Palavras-chave: HOMOBASIDIOMYCOTA; HOMOBASIDIOMYCETE; SSU-RRNA; DOMAINE VARIABLE HOMOBASIDIOMYCOTA; MUSHROOM; MITOCHONDRIA; SSU-RRNA; VARIABLE DOMAINS; INSERTION/DELETION; HAIRPIN. |
| Ano: 2003 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0400012024100763&uri=/notices/prodinra1/2010/12/ |
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| Boxma, B.; Ricard, G.; van Hoek, A. H.; Severing, E.; Moon-van der Staay, S.Y.; van der Staay, G.W.M.; van Alen, T.A.; de Graaf, R.M.; Cremers, G.; Kwantes, M.; McEwan, N.R.; Newbold, C.J.; Jouany, J.P.; Michalowski, T.; Pristas, P.; Huynen, M.A.; Hackstein, J.H.P.. |
| Background: The hydrogenosomes of the anaerobic ciliate Nyctotherus ovalis show how mitochondria can evolve into hydrogenosomes because they possess a mitochondrial genome and parts of an electron-transport chain on the one hand, and a hydrogenase on the other hand. The hydrogenase permits direct reoxidation of NADH because it consists of a [ FeFe] hydrogenase module that is fused to two modules, which are homologous to the 24 kDa and the 51 kDa subunits of a mitochondrial complex I.Results: The [ FeFe] hydrogenase belongs to a clade of hydrogenases that are different from well-known eukaryotic hydrogenases. The 24 kDa and the 51 kDa modules are most closely related to homologous modules that function in bacterial [ NiFe] hydrogenases. Paralogous,... |
| Tipo: Journal Article |
Palavras-chave: MITOCHONDRIE; CILIE; HYDROGENASE MULTIPLE SEQUENCE ALIGNMENT; COMPLEX-I; PHYLOGENETIC ANALYSIS; EUKARYOTIC EVOLUTION; IRON HYDROGENASES; LIFE-STYLE; HYDROGENOSOMES; MITOCHONDRIA; PROTEIN; MODELS. |
| Ano: 2007 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2008786cfe28&uri=/notices/prodinra1/2009/10/ |
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