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Pesquisa : D12.776.157.530.450.074.750 [Categoria DeCS]
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[PMID]:28968924
[Au] Autor:Zvobgo G; LwalabaWaLwalaba J; Sagonda T; Mutemachani Mapodzeke J; Muhammad N; Haider Shamsi I; Zhang G
[Ad] Endereço:Department of Agronomy, College of Agriculture and Biotechnology, Key Laboratory of Crop Germplasm Resource, Zhejiang University, Hangzhou 310058, PR China.
[Ti] Título:Phosphate alleviates arsenate toxicity by altering expression of phosphate transporters in the tolerant barley genotypes.
[So] Source:Ecotoxicol Environ Saf;147:832-839, 2018 Jan.
[Is] ISSN:1090-2414
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The contribution of the phosphate transporters (PHTs) in uptake of arsenate (As ) and phosphate (P) is a widely recognized mechanism. Here we investigated how P regulates the uptake of As and the subsequent effects on growth and relative expression of PHTs. The study was conducted on 3 barley genotypes differing in As tolerance (ZDB160, As-tolerant; ZDB115, moderately tolerant; ZDB475, As-sensitive) using a hydroponic experiment. There were 3 As (0, 10 and 100µM) and 3P (0, 50 and 500µM) levels. The results showed that the negative effect of As stress on plant growth, photosynthesis and cell ultra-structure is As dose and barley genotype dependent, confirming the distinctly genotypic difference in As tolerance. As uptake and accumulation in plant tissues are closely associated with inhibited extent of growth and photosynthesis, with the tolerant genotype ZDB160 having lower As content than other two genotypes. The toxic effect caused by As stress could be alleviated by P addition, mainly due to reduced As uptake. Moreover, the tolerant genotype showed relatively lower expression PHTs than sensitive ones upon exposure to both As stress and P addition, suggesting regulation of PHTs expression is a major mechanism for relative uptake of As and P, in subsequence affecting As tolerance. Moreover, among 6 PHTs examined in this study, the expressions of PHT1.3, PHT1.4 and PHT1.6 showed the marked difference among the three barley genotypes in responses to As stress and P addition, indicating further research on the contribution of phosphate transporters to As and P uptake should be focused on these PHTs.
[Mh] Termos MeSH primário: Adaptação Biológica
Arseniatos/toxicidade
Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Hordeum/metabolismo
Proteínas de Transporte de Fosfato/genética
Fosfatos/farmacologia
Poluentes do Solo/toxicidade
[Mh] Termos MeSH secundário: Adaptação Biológica/genética
Arseniatos/metabolismo
Biomassa
Genótipo
Hordeum/genética
Hordeum/crescimento & desenvolvimento
Modelos Teóricos
Fosfatos/metabolismo
Fotossíntese/efeitos dos fármacos
Poluentes do Solo/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arsenates); 0 (Phosphate Transport Proteins); 0 (Phosphates); 0 (Soil Pollutants)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171004
[St] Status:MEDLINE


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[PMID]:28376086
[Au] Autor:Terzenidou ME; Segklia A; Kano T; Papastefanaki F; Karakostas A; Charalambous M; Ioakeimidis F; Papadaki M; Kloukina I; Chrysanthou-Piterou M; Samiotaki M; Panayotou G; Matsas R; Douni E
[Ad] Endereço:Laboratory of Genetics, Department of Biotechnology, Agricultural University of Athens, Athens, Greece.
[Ti] Título:Novel insights into SLC25A46-related pathologies in a genetic mouse model.
[So] Source:PLoS Genet;13(4):e1006656, 2017 Apr.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mitochondrial protein SLC25A46 has been recently identified as a novel pathogenic cause in a wide spectrum of neurological diseases, including inherited optic atrophy, Charcot-Marie-Tooth type 2, Leigh syndrome, progressive myoclonic ataxia and lethal congenital pontocerebellar hypoplasia. SLC25A46 is an outer membrane protein, member of the Solute Carrier 25 (SLC25) family of nuclear genes encoding mitochondrial carriers, with a role in mitochondrial dynamics and cristae maintenance. Here we identified a loss-of-function mutation in the Slc25a46 gene that causes lethal neuropathology in mice. Mutant mice manifest the main clinical features identified in patients, including ataxia, optic atrophy and cerebellar hypoplasia, which were completely rescued by expression of the human ortholog. Histopathological analysis revealed previously unseen lesions, most notably disrupted cytoarchitecture in the cerebellum and retina and prominent abnormalities in the neuromuscular junction. A distinct lymphoid phenotype was also evident. Our mutant mice provide a valid model for understanding the mechanistic basis of the complex SLC25A46-mediated pathologies, as well as for screening potential therapeutic interventions.
[Mh] Termos MeSH primário: Doença de Charcot-Marie-Tooth/genética
Mitocôndrias/genética
Proteínas Mitocondriais/genética
Mutação/genética
Proteínas de Transporte de Fosfato/genética
[Mh] Termos MeSH secundário: Animais
Ataxia/genética
Ataxia/fisiopatologia
Doenças Cerebelares/genética
Doenças Cerebelares/fisiopatologia
Doença de Charcot-Marie-Tooth/patologia
Modelos Animais de Doenças
Seres Humanos
Camundongos
Camundongos Knockout
Mitocôndrias/patologia
Membranas Mitocondriais/metabolismo
Atrofia Óptica/genética
Atrofia Óptica/fisiopatologia
Linhagem
Fenótipo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mitochondrial Proteins); 0 (Phosphate Transport Proteins); 0 (SLC25A46 protein, human)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170517
[Lr] Data última revisão:
170517
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170405
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006656


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[PMID]:28376083
[Au] Autor:Duchesne A; Vaiman A; Castille J; Beauvallet C; Gaignard P; Floriot S; Rodriguez S; Vilotte M; Boulanger L; Passet B; Albaric O; Guillaume F; Boukadiri A; Richard L; Bertaud M; Timsit E; Guatteo R; Jaffrézic F; Calvel P; Helary L; Mahla R; Esquerré D; Péchoux C; Liuu S; Vallat JM; Boichard D; Slama A; Vilotte JL
[Ad] Endereço:GABI, INRA, AgroParisTech, Université Paris-Saclay, Jouy-en-Josas, France.
[Ti] Título:Bovine and murine models highlight novel roles for SLC25A46 in mitochondrial dynamics and metabolism, with implications for human and animal health.
[So] Source:PLoS Genet;13(4):e1006597, 2017 Apr.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neuropathies are neurodegenerative diseases affecting humans and other mammals. Many genetic causes have been identified so far, including mutations of genes encoding proteins involved in mitochondrial dynamics. Recently, the "Turning calves syndrome", a novel sensorimotor polyneuropathy was described in the French Rouge-des-Prés cattle breed. In the present study, we determined that this hereditary disease resulted from a single nucleotide substitution in SLC25A46, a gene encoding a protein of the mitochondrial carrier family. This mutation caused an apparent damaging amino-acid substitution. To better understand the function of this protein, we knocked out the Slc25a46 gene in a mouse model. This alteration affected not only the nervous system but also altered general metabolism, resulting in premature mortality. Based on optic microscopy examination, electron microscopy and on biochemical, metabolic and proteomic analyses, we showed that the Slc25a46 disruption caused a fusion/fission imbalance and an abnormal mitochondrial architecture that disturbed mitochondrial metabolism. These data extended the range of phenotypes associated with Slc25a46 dysfunction. Moreover, this Slc25a46 knock-out mouse model should be useful to further elucidate the role of SLC25A46 in mitochondrial dynamics.
[Mh] Termos MeSH primário: Dinâmica Mitocondrial/genética
Proteínas Mitocondriais/genética
Proteínas de Transporte de Fosfato/genética
Polineuropatias/genética
Proteômica
[Mh] Termos MeSH secundário: Substituição de Aminoácidos/genética
Animais
Bovinos
Seres Humanos
Camundongos
Mitocôndrias/genética
Mitocôndrias/patologia
Mutação
Fenótipo
Polineuropatias/patologia
Polineuropatias/veterinária
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mitochondrial Proteins); 0 (Phosphate Transport Proteins); 0 (SLC25A46 protein, human)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170517
[Lr] Data última revisão:
170517
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170405
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006597


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[PMID]:28286238
[Au] Autor:Minashima T; Quirno M; Lee YJ; Kirsch T
[Ad] Endereço:Musculoskeletal Research Center, Department of Orthopaedic Surgery, New York University School of Medicine, NY, New York, United States.
[Ti] Título:The role of the progressive ankylosis protein (ANK) in adipogenic/osteogenic fate decision of precursor cells.
[So] Source:Bone;98:38-46, 2017 May.
[Is] ISSN:1873-2763
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The progressive ankylosis protein (ANK) is a transmembrane protein that transports intracellular pyrophosphate (PPi) to the extracellular milieu. In this study we show increased fatty degeneration of the bone marrow of adult ank/ank mice, which lack a functional ANK protein. In addition, isolated bone marrow stromal cells (BMSCs) isolated from ank/ank mice showed a decreased proliferation rate and osteogenic differentiation potential, and an increased adipogenic differentiation potential compared to BMSCs isolated from wild type (WT) littermates. Wnt signaling pathway PCR array analysis revealed that Wnt ligands, Wnt receptors and Wnt signaling proteins that stimulate osteoblast differentiation were expressed at markedly lower levels in ank/ank BMSCs than in WT BMSCs. Lack of ANK function also resulted in impaired bone fracture healing, as indicated by a smaller callus formed and delayed bone formation in the callus site. Whereas 5weeks after fracture, the fractured bone in WT mice was further remodeled and restored to original shape, the fractured bone in ank/ank mice was not fully restored and remodeled to original shape. In conclusion, our study provides evidence that ANK plays a critical role in the adipogenic/osteogenic fate decision of adult mesenchymal precursor cells. ANK functions in precursor cells are required for osteogenic differentiation of these cells during adult bone homeostasis and repair, whereas lack of ANK functions favors adipogenic differentiation.
[Mh] Termos MeSH primário: Adipogenia/fisiologia
Diferenciação Celular/fisiologia
Células Mesenquimais Estromais/citologia
Osteogênese/fisiologia
Proteínas de Transporte de Fosfato/metabolismo
[Mh] Termos MeSH secundário: Adipócitos/citologia
Adipócitos/metabolismo
Animais
Medula Óssea/patologia
Feminino
Masculino
Camundongos
Camundongos Mutantes
Osteócitos/citologia
Osteócitos/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Via de Sinalização Wnt/fisiologia
Microtomografia por Raio-X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phosphate Transport Proteins); 0 (ank protein, mouse)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170427
[Lr] Data última revisão:
170427
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170314
[St] Status:MEDLINE


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[PMID]:28224717
[Au] Autor:Sugahara R; Jouraku A; Nakakura T; Minaba M; Yamamoto T; Shinohara Y; Miyoshi H; Shiotsuki T
[Ad] Endereço:National Agriculture and Food Research Organization, Institute of Agrobiological Sciences, 1-2 Owashi, Tsukuba, Ibaraki, Japan.
[Ti] Título:Tissue-specific expression and silencing phenotypes of mitochondrial phosphate carrier paralogues in several insect species.
[So] Source:Insect Mol Biol;26(3):332-342, 2017 Jun.
[Is] ISSN:1365-2583
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The mitochondrial phosphate carrier gene (PiC) encodes a membrane protein that mediates the supply of inorganic phosphate from the cytosol into the mitochondrial matrix. This substrate-specific transport system plays an important role in efficient ATP synthesis. Mammals appear to have only one PiC with two alternative splicing variants whose functional differences remain unclear. The present study is the first to characterize the multiple genes that encode PiC in insects. Bombyx mori was found to have two PiC paralogues, one ubiquitous and one testis-specific, the latter seeming to be present only in Lepidoptera. Drosophila melanogaster was found to harbour two PiC paralogues, whereas Liriomyza chinensis, another dipteran, has three PiC paralogues. Two PiCs were found to be present in Plautia stali, and silencing either of these genes affected the normal development of P. stali nymphs, although their expression patterns differed amongst tissues. Schistocerca gregaria and Locusta migratoria have two PiC each, with different expression patterns. Tribolium castaneum was found to have only one PiC, which appears to play an essential role in larval development. Thus, although the inorganic phosphate transport system appears to be conserved across eukaryotes, PiC has become specialized in the different tissues of different insect species.
[Mh] Termos MeSH primário: Proteínas de Insetos/metabolismo
Insetos/metabolismo
Proteínas Mitocondriais/metabolismo
Proteínas de Transporte de Fosfato/metabolismo
[Mh] Termos MeSH secundário: Animais
Feminino
Proteínas de Insetos/genética
Insetos/genética
Masculino
Proteínas Mitocondriais/genética
Músculos/metabolismo
Proteínas de Transporte de Fosfato/genética
Filogenia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insect Proteins); 0 (Mitochondrial Proteins); 0 (Phosphate Transport Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170223
[St] Status:MEDLINE
[do] DOI:10.1111/imb.12297


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[PMID]:28207830
[Au] Autor:Tian H; Yuan X; Duan J; Li W; Zhai B; Gao Y
[Ad] Endereço:Key Laboratory of Plant Nutrition and Agri-environment in Northwest China, Ministry of Agriculture, College of Natural Resources and Environment, Northwest A&F University, Yangling, Shaanxi, China.
[Ti] Título:Influence of nutrient signals and carbon allocation on the expression of phosphate and nitrogen transporter genes in winter wheat (Triticum aestivum L.) roots colonized by arbuscular mycorrhizal fungi.
[So] Source:PLoS One;12(2):e0172154, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Arbuscular mycorrhizal (AM) colonization of plant roots causes the down-regulation of expression of phosphate (Pi) or nitrogen (N) transporter genes involved in direct nutrient uptake pathways. The mechanism of this effect remains unknown. In the present study, we sought to determine whether the expression of Pi or N transporter genes in roots of winter wheat colonized by AM fungus responded to (1) Pi or N nutrient signals transferred from the AM extra-radical hyphae, or (2) carbon allocation changes in the AM association. A three-compartment culture system, comprising a root compartment (RC), a root and AM hyphae compartment (RHC), and an AM hyphae compartment (HC), was used to test whether the expression of Pi or N transporter genes responded to nutrients (Pi, NH4+ and NO3-) added only to the HC. Different AM inoculation density treatments (roots were inoculated with 0, 20, 50 and 200 g AM inoculum) and light regime treatments (6 hours light and 18 hours light) were established to test the effects of carbon allocation on the expression of Pi or N transporter genes in wheat roots. The expression of two Pi transporter genes (TaPT4 and TaPHT1.2), five nitrate transporter genes (TaNRT1.1, TaNRT1.2, TaNRT2.1, TaNRT2.2, and TaNRT2.3), and an ammonium transporter gene (TaAMT1.2) was quantified using real-time polymerase chain reaction. The expression of TaPT4, TaNRT2.2, and TaAMT1.2 was down-regulated by AM colonization only when roots of host plants received Pi or N nutrient signals. However, the expression of TaPHT1.2, TaNRT2.1, and TaNRT2.3 was down-regulated by AM colonization, regardless of whether there was nutrient transfer from AM hyphae. The expression of TaNRT1.2 was also down-regulated by AM colonization even when there was no nutrient transfer from AM hyphae. The present study showed that an increase in carbon consumption by the AM fungi did not necessarily result in greater down-regulation of expression of Pi or N transporter genes.
[Mh] Termos MeSH primário: Carbono/metabolismo
Micorrizas/fisiologia
Nitrogênio/metabolismo
Proteínas de Transporte de Fosfato/genética
Fosfatos/metabolismo
Proteínas de Plantas/genética
Raízes de Plantas/microbiologia
Triticum/microbiologia
[Mh] Termos MeSH secundário: Alimentos
Regulação da Expressão Gênica de Plantas
Raízes de Plantas/genética
Raízes de Plantas/crescimento & desenvolvimento
Simbiose
Triticum/genética
Triticum/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phosphate Transport Proteins); 0 (Phosphates); 0 (Plant Proteins); 7440-44-0 (Carbon); N762921K75 (Nitrogen)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170217
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0172154


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[PMID]:28057766
[Au] Autor:Steffen J; Vashisht AA; Wan J; Jen JC; Claypool SM; Wohlschlegel JA; Koehler CM
[Ad] Endereço:Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095.
[Ti] Título:Rapid degradation of mutant SLC25A46 by the ubiquitin-proteasome system results in MFN1/2-mediated hyperfusion of mitochondria.
[So] Source:Mol Biol Cell;28(5):600-612, 2017 Mar 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:SCL25A46 is a mitochondrial carrier protein that surprisingly localizes to the outer membrane and is distantly related to Ugo1. Here we show that a subset of SLC25A46 interacts with mitochondrial dynamics components and the MICOS complex. Decreased expression of SLC25A46 results in increased stability and oligomerization of MFN1 and MFN2 on mitochondria, promoting mitochondrial hyperfusion. A mutation at L341P causes rapid degradation of SLC25A46, which manifests as a rare disease, pontocerebellar hypoplasia. The E3 ubiquitin ligases MULAN and MARCH5 coordinate ubiquitylation of SLC25A46 L341P, leading to degradation by organized activities of P97 and the proteasome. Whereas outer mitochondrial membrane-associated degradation is typically associated with apoptosis or a specialized type of autophagy termed mitophagy, SLC25A46 degradation operates independently of activation of outer membrane stress pathways. Thus SLC25A46 is a new component in mitochondrial dynamics that serves as a regulator for MFN1/2 oligomerization. Moreover, SLC25A46 is selectively degraded from the outer membrane independently of mitophagy and apoptosis, providing a framework for mechanistic studies in the proteolysis of outer membrane proteins.
[Mh] Termos MeSH primário: GTP Fosfo-Hidrolases/metabolismo
Dinâmica Mitocondrial/fisiologia
Proteínas de Transporte da Membrana Mitocondrial/metabolismo
Proteínas Mitocondriais/metabolismo
Proteínas de Transporte de Fosfato/metabolismo
[Mh] Termos MeSH secundário: Apoptose/fisiologia
Autofagia/fisiologia
Células HEK293
Células HeLa
Seres Humanos
Mitocôndrias/metabolismo
Membranas Mitocondriais/metabolismo
Complexo de Endopeptidases do Proteassoma/metabolismo
Proteólise
Ubiquitina/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mitochondrial Membrane Transport Proteins); 0 (Mitochondrial Proteins); 0 (Phosphate Transport Proteins); 0 (SLC25A46 protein, human); 0 (Ubiquitin); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 3.4.25.1 (Proteasome Endopeptidase Complex); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (MFN2 protein, human); EC 3.6.5.- (Mfn1 protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170107
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-07-0545


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[PMID]:27836624
[Au] Autor:Yamagoshi R; Yamamoto T; Hashimoto M; Sugahara R; Shiotsuki T; Miyoshi H; Terada H; Shinohara Y
[Ad] Endereço:Institute for Genome Research, Tokushima University, Kuramotocho-3, Tokushima 770-8503, Japan; Faculty of Pharmaceutical Sciences, Tokushima University, Shomachi-1, Tokushima 770-8505, Japan.
[Ti] Título:Identification of amino acid residues of mammalian mitochondrial phosphate carrier important for its functional expression in yeast cells, as achieved by PCR-mediated random mutation and gap-repair cloning.
[So] Source:Mitochondrion;32:1-9, 2017 Jan.
[Is] ISSN:1872-8278
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The mitochondrial phosphate carrier (PiC) of mammals, but not the yeast one, is synthesized with a presequence. The deletion of this presequence of the mammalian PiC was reported to facilitate the import of the carrier into yeast mitochondria, but the question as to whether or not mammalian PiC could be functionally expressed in yeast mitochondria was not addressed. In the present study, we first examined whether the defective growth on a glycerol plate of yeast cells lacking the yeast PiC gene could be reversed by the introduction of expression vectors of rat PiCs. The introduction of expression vectors encoding full-length rat PiC (rPiC) or rPiC lacking the presequence (ΔNrPiC) was ineffective in restoring growth on the glycerol plates. When we examined the expression levels of individual rPiCs in yeast mitochondria, ΔNrPiC was expressed at a level similar to that of yeast PiC, but that of rPiC was very low. These results indicated that ΔNrPiC expressed in yeast mitochondria is inert. Next, we sought to isolate "revertants" viable on the glycerol plate by expressing randomly mutated ΔNrPiC, and obtained two clones. These clones carried either of two mutations, F267S or F282S; and these mutations restored the transport function of ΔNrPiC in yeast mitochondria. These two Phe residues were conserved in human carrier (hPiC), and the transport function of ΔNhPiC expressed in yeast mitochondria was also markedly improved by their substitutions. Thus, substitution of F267S or F282S was concluded to be important for functional expression of mammalian PiCs in yeast mitochondria.
[Mh] Termos MeSH primário: Clonagem Molecular
Expressão Gênica
Proteínas de Transporte de Fosfato/biossíntese
Proteínas de Transporte de Fosfato/genética
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/genética
Saccharomyces cerevisiae/enzimologia
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Animais
Meios de Cultura/química
Análise Mutacional de DNA
Glicerol/metabolismo
Mutagênese
Reação em Cadeia da Polimerase/métodos
Ratos
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Culture Media); 0 (Phosphate Transport Proteins); 0 (Recombinant Proteins); PDC6A3C0OX (Glycerol)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170508
[Lr] Data última revisão:
170508
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161113
[St] Status:MEDLINE


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[PMID]:26951855
[Au] Autor:Nguyen M; Boesten I; Hellebrekers DM; Mulder-den Hartog NM; de Coo IF; Smeets HJ; Gerards M
[Ad] Endereço:Department of Clinical Genetics, Unit Clinical Genomics, Maastricht University Medical Centre, Maastricht, The Netherlands.
[Ti] Título:Novel pathogenic SLC25A46 splice-site mutation causes an optic atrophy spectrum disorder.
[So] Source:Clin Genet;91(1):121-125, 2017 Jan.
[Is] ISSN:1399-0004
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Ab] Resumo:The inherited optic neuropathies comprise a group of genetically heterogeneous disorders causing optic nerve dysfunction. In some cases, optic neuropathies are associated with cerebellar atrophy which mainly affects the vermis. Here, we describe a Moroccan girl of consanguineous parents with optic atrophy and cerebellar atrophy. Exome sequencing revealed a novel homozygous mutation (c.283+3G>T) in the donor splice site for exon 1 of SLC25A46. RNA analysis revealed that an alternative splice site within exon 1 was used leading to a premature termination codon within exon 2. SLC25A46 mRNA expression showed there is no wild-type transcript present in the patient and the mutant transcript does not undergo nonsense-mediated mRNA decay. Futhermore, we observed c.283+3G>T SLC25A46 mutation induces mitochondrial fragmentation. An additional 10 patients with optic atrophy and cerebellar atrophy, which were negative for mtDNA and OPA1 variants, were tested for pathogenic mutations in the SLC25A46 gene. However, no additional variants were identified. Our findings confirm the recent report of pathogenic SLC25A46 mutations as a novel cause for optic atrophy spectrum disorder.
[Mh] Termos MeSH primário: Predisposição Genética para Doença/genética
Proteínas Mitocondriais/genética
Mutação
Atrofias Ópticas Hereditárias/genética
Proteínas de Transporte de Fosfato/genética
Sítios de Splice de RNA/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Consanguinidade
Exoma/genética
Éxons/genética
Saúde da Família
Feminino
Seres Humanos
Masculino
Pais
Linhagem
Análise de Sequência de DNA/métodos
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mitochondrial Proteins); 0 (Phosphate Transport Proteins); 0 (RNA Splice Sites); 0 (SLC25A46 protein, human)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170613
[Lr] Data última revisão:
170613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160309
[St] Status:MEDLINE
[do] DOI:10.1111/cge.12774


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[PMID]:27911737
[Au] Autor:Ceasar SA; Baker A; Muench SP; Ignacimuthu S; Baldwin SA
[Ad] Endereço:Division of Plant Biotechnology, Entomology Research Institute, Loyola College, Chennai 600034, India.
[Ti] Título:The conservation of phosphate-binding residues among PHT1 transporters suggests that distinct transport affinities are unlikely to result from differences in the phosphate-binding site.
[So] Source:Biochem Soc Trans;44(5):1541-1548, 2016 Oct 15.
[Is] ISSN:1470-8752
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The plant PHosphate Transporter 1 (PHT1) family of membrane proteins belongs to the major facilitator super family and plays a major role in the acquisition of inorganic phosphate (Pi) from the soil and its transport within the plant. These transporters have been well characterized for expression patterns, localization, and in some cases affinity. Furthermore, the crystal structure of a high-affinity eukaryotic phosphate transporter from the fungus Piriformospora indica (PiPT) has revealed important information on the residues involved in Pi transport. Using multiple-sequence alignments and homology modelling, the phosphate-binding site residues were shown to be well conserved between all the plant PHT1 proteins, Saccharomyces cerevisiae PHO84 and PiPT. For example, Asp 324 in PiPT is conserved in the equivalent position in all plant PHT1 and yeast transporters analyzed, and this residue in ScPHO84 was shown by mutagenesis to be important for both the binding and transport of Pi. Moreover, Asp 45 and Asp 149, which are predicted to be involved in proton import, and Lys 459, which is putatively involved in Pi-binding, are all fully conserved in PHT1 and ScPHO84 transporters. The conserved nature of the residues that play a key role in Pi-binding and transport across the PHT1 family suggests that the differing Pi affinities of these transporters do not reside in differences in the Pi-binding site. Recent studies suggest that phosphate transporters could possess dual affinity and that post-translational modifications may be important in regulating affinity for phosphate.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Proteínas de Transporte de Fosfato/metabolismo
Fosfatos/metabolismo
Simportadores de Próton-Fosfato/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Arabidopsis/genética
Sequência de Bases
Sítios de Ligação/genética
Ligação Competitiva
Evolução Molecular
Proteínas de Transporte de Fosfato/genética
Ligação Proteica
Simportadores de Próton-Fosfato/genética
Proteínas de Saccharomyces cerevisiae/genética
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (PHO84 protein, S cerevisiae); 0 (PHT1;1 protein, Arabidopsis); 0 (Phosphate Transport Proteins); 0 (Phosphates); 0 (Proton-Phosphate Symporters); 0 (Saccharomyces cerevisiae Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161203
[St] Status:MEDLINE



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