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[PMID]:28471359
[Au] Autor:Han W; Cheng J; Zhou C; Hua Y; Zhao Y
[Ad] Endereço:Key Laboratory of Chinese Ministry of Agriculture for Nuclear-Agricultural Sciences, Institute of Nuclear-Agricultural Sciences, Zhejiang University, People's Republic of China.
[Ti] Título:Crystal structure of the RNA 2',3'-cyclic phosphodiesterase from Deinococcus radiodurans.
[So] Source:Acta Crystallogr F Struct Biol Commun;73(Pt 5):276-280, 2017 May 01.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:2',3'-Cyclic phosphodiesterase (CPDase) homologues have been found in all domains of life and are involved in diverse RNA and nucleotide metabolisms. The CPDase from Deinococcus radiodurans was crystallized and the crystals diffracted to 1.6 Šresolution, which is the highest resolution currently known for a CPDase structure. Structural comparisons revealed that the enzyme is in an open conformation in the absence of substrate. Nevertheless, the active site is well formed, and the representative motifs interact with sulfate ion, which suggests a conserved catalytic mechanism.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Deinococcus/química
Nucleotidases/química
RNA Bacteriano/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Domínio Catalítico
Clonagem Molecular
Cristalografia por Raios X
Deinococcus/enzimologia
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Vetores Genéticos/química
Vetores Genéticos/metabolismo
Modelos Moleculares
Nucleotidases/genética
Nucleotidases/metabolismo
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
RNA Bacteriano/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (RNA, Bacterial); 0 (Recombinant Proteins); EC 3.1.3.- (Nucleotidases); EC 3.1.3.6 (3'-nucleotidase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171204
[Lr] Data última revisão:
171204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X17004964


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[PMID]:28742282
[Au] Autor:Balasubramanian K; Li B; Krakow D; Nevarez L; Ho PJ; Ainsworth JA; Nickerson DA; Bamshad MJ; Immken L; Lachman RS; Cohn DH
[Ad] Endereço:Department of Molecular, Cell and Developmental Biology, University of California Los Angeles, Los Angeles, California.
[Ti] Título:MED resulting from recessively inherited mutations in the gene encoding calcium-activated nucleotidase CANT1.
[So] Source:Am J Med Genet A;173(9):2415-2421, 2017 Sep.
[Is] ISSN:1552-4833
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Multiple Epiphyseal Dysplasia (MED) is a relatively mild skeletal dysplasia characterized by mild short stature, joint pain, and early-onset osteoarthropathy. Dominantly inherited mutations in COMP, MATN3, COL9A1, COL9A2, and COL9A3, and recessively inherited mutations in SLC26A2, account for the molecular basis of disease in about 80-85% of the cases. In two families with recurrent MED of an unknown molecular basis, we used exome sequencing and candidate gene analysis to identify homozygosity for recessively inherited missense mutations in CANT1, which encodes calcium-activated nucleotidase 1. The MED phenotype is thus allelic to the more severe Desbuquois dysplasia phenotype and the results identify CANT1 as a second locus for recessively inherited MED.
[Mh] Termos MeSH primário: Genes Recessivos
Nucleotidases/genética
Osteocondrodisplasias/genética
[Mh] Termos MeSH secundário: Adulto
Sequência de Bases
Criança
Pré-Escolar
Exoma/genética
Feminino
Seres Humanos
Masculino
Mutação de Sentido Incorreto/genética
Osteocondrodisplasias/diagnóstico por imagem
Osteocondrodisplasias/fisiopatologia
Linhagem
Radiografia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.1.3.- (CANT1 protein, human); EC 3.1.3.- (Nucleotidases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171130
[Lr] Data última revisão:
171130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1002/ajmg.a.38349


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[PMID]:28717030
[Au] Autor:Kao DJ; Saeedi BJ; Kitzenberg D; Burney KM; Dobrinskikh E; Battista KD; Vázquez-Torres A; Colgan SP; Kominsky DJ
[Ad] Endereço:Mucosal Inflammation Program, University of Colorado Anschutz Medical Campus, Aurora, Colorado, USA.
[Ti] Título:Intestinal Epithelial Ecto-5'-Nucleotidase (CD73) Regulates Intestinal Colonization and Infection by Nontyphoidal Salmonella.
[So] Source:Infect Immun;85(10), 2017 Oct.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ecto-5'-nucleotidase (CD73) is expressed abundantly on the apical surface of intestinal epithelial cells (IECs) and functions as the terminal enzyme in the generation of extracellular adenosine. Previous work demonstrated that adenosine signaling in IECs results in a number of tissue-protective effects during inflammation; however, a rationale for its apical expression has been lacking. We hypothesized that the highly polarized expression of CD73 is indicative of an important role for extracellular adenosine as a mediator of host-microbe interactions. We show that adenosine harbors bacteriostatic activity against serovar Typhimurium that is not shared by the related purine metabolite 5'-AMP, inosine, or hypoxanthine. Analysis of colonization in IEC-specific CD73 knockout mice ( ) revealed a nearly 10-fold increase in colonization compared to that in controls. Despite the increased luminal colonization by , mice were protected against colitis and showed reduced burdens in viscera, suggesting that adenosine promotes dissemination. The knockdown of CD73 expression in cultured IECs resulted in dramatic defects in intraepithelial localization and replication as well as defective transepithelial translocation by In conclusion, we define a novel antimicrobial activity of adenosine in the gastrointestinal tract and unveil an important role for adenosine as a regulator of host-microbe interactions. These findings have broad implications for the development of new therapeutic agents for infectious disease.
[Mh] Termos MeSH primário: 5´-Nucleotidase/metabolismo
Adenosina/metabolismo
Interações Hospedeiro-Patógeno
Mucosa Intestinal/microbiologia
Salmonella enterica/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: 5'-Nucleotidase/deficiência
5'-Nucleotidase/genética
Adenosina/imunologia
Animais
Carga Bacteriana
Linhagem Celular
Células Epiteliais/microbiologia
Inflamação
Camundongos
Camundongos Knockout
Nucleotidases/metabolismo
Salmonella enterica/fisiologia
Salmonella typhimurium/crescimento & desenvolvimento
Salmonella typhimurium/fisiologia
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.1.3.- (Nucleotidases); EC 3.1.3.31 (nucleotidase); EC 3.1.3.5 (5'-Nucleotidase); K72T3FS567 (Adenosine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170719
[St] Status:MEDLINE


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[PMID]:28710007
[Au] Autor:Doleski PH; Ten Caten MV; Passos DF; Castilhos LG; Leal DBR; Machado VS; Bottari NB; Vogel FF; Mendes RE; da Silva AS
[Ad] Endereço:Department of Microbiology and Parasitology, Universidade Federal de Santa Maria (UFSM), Brazil; Department of Biochemistry and Molecular Biology, Universidade Federal de Santa Maria (UFSM), Brazil.
[Ti] Título:Toxoplasmosis treatment with diphenyl diselenide in infected mice modulates the activity of purinergic enzymes and reduces inflammation in spleen.
[So] Source:Exp Parasitol;181:7-13, 2017 Oct.
[Is] ISSN:1090-2449
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Toxoplasma gondii, an intracellular protozoan, may cause chronic infection in the brain tissue of the host inducing a systemic pro-inflammatory profile. Chronic infections can induce numerous physiological changes, such as alterations in the immune and oxidative profiles. Diphenyl diselenide (PhSe) , an organoselenium compound, has shown antioxidant and immunomodulatory activities in recent studies. So, the aim of this study was to investigate the activity of purinergic enzymes and reactive oxygen species (ROS) in serum and spleen of mice chronically infected by T. gondii, untreated and treated with (PhSe) . For this experiment, were divided into four groups: Group A (healthy mice), Group B (healthy mice treated with (PhSe) ), Group C (infected mice) and Group D (infected mice treated with (PhSe) ). Group C and group D were infected via oral route with ME49 Toxoplasma gondii strain. Groups B and D were treated subcutaneously with 5 µmol kg of (PhSe) . Chronic T. gondii infection induced splenomegaly and physiological changes in the spleen and raised histologic inflammatory markers, ROS levels and the activity of purinergic enzymes activity such as NTPDase, 5´nucleotidase and ADA. In serum, the infection increased 5´nucleotidase and ADA activities. (PhSe) per se has managed to decrease ROS levels and ADA activity and increase NTPDase and 5´nucleotidase in spleen. In infected mice, treatment with (PhSe) reversed splenomegaly, reduced histological inflammatory markers, ROS levels and ADA activity in the spleen. Our results prove that chronic toxoplasmosis can induce splenomegaly, heightens ROS levels and purinergic enzyme activity in mice. These results suggest that (PhSe) is a potential therapy for the alterations found in the spleen in chronic T. gondii infection.
[Mh] Termos MeSH primário: Derivados de Benzeno/uso terapêutico
Nucleotidases/sangue
Compostos Organosselênicos/uso terapêutico
Baço/patologia
Toxoplasmose Animal/tratamento farmacológico
[Mh] Termos MeSH secundário: 5'-Nucleotidase/sangue
5'-Nucleotidase/metabolismo
Difosfato de Adenosina/metabolismo
Trifosfato de Adenosina/metabolismo
Animais
Derivados de Benzeno/farmacologia
Feminino
Inflamação/tratamento farmacológico
Camundongos
Nucleotidases/metabolismo
Compostos Organosselênicos/farmacologia
Espécies Reativas de Oxigênio/sangue
Espécies Reativas de Oxigênio/metabolismo
Baço/efeitos dos fármacos
Baço/enzimologia
Baço/metabolismo
Toxoplasmose Animal/enzimologia
Toxoplasmose Animal/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzene Derivatives); 0 (Organoselenium Compounds); 0 (Reactive Oxygen Species); 1666-13-3 (diphenyldiselenide); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 3.1.3.- (Nucleotidases); EC 3.1.3.5 (5'-Nucleotidase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170716
[St] Status:MEDLINE


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[PMID]:28628836
[Au] Autor:Liu Y; Sun MH; Shao SK; Deng G
[Ad] Endereço:College of Chemistry and Life Sciences, Zhejiang Normal University, Jinhua 321004, China.
[Ti] Título:An affinity-based aqueous two-phase mixed micellar system and its purification of Yeast 3',5'-bisphosphate nucleotidase.
[So] Source:J Chromatogr B Analyt Technol Biomed Life Sci;1060:215-220, 2017 Aug 15.
[Is] ISSN:1873-376X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Aqueous two-phase micellar system (ATPMS), as an alternative liquid-liquid extraction technique, has been extensively exploited for the precise separation or large-scale concentration of biomolecules. In this article, a novel affinity-based ATPMS composed of mixed micelles was constructed by introducing a Copper-chelated Triton X-114 (TX-Cu(II)) into an aqueous solution of hydrophobically modified ethylene oxide polymer (HM-EO). Phase diagram of the HM-EO/TX-Cu(II) system was measured, and the partitioning behavior of model proteins (YND, BSA, lysozyme) were studied by using this new system. The addition of HM-EO can result in formation of the micellar network in the micelle-rich phase, making the phase separation easier and stabler. In addition, the extractive performance of ATPMS was enhanced due to the existence of the mixed micelles composed by HM-EO and Cu(II)-chelated TX. It was found in the partitioning experiments that the hexahistidine-tagged Yeast 3',5'-bisphosphate nucleotidase (YND) was selectively extracted into the micelle-rich phase, while the histidine-poor proteins (BSA and lysozyme) remained in the micelle-poor phase. Finally, HM-EO/TX-Cu(II) was used directly to process the fermentation broth. The target protein, YND could be recovered from the cell lysate with a recovery yield of 49.23% and purification factor of 2.63. The results indicated that the new affinity-based HM-EO/TX-Cu(II) system had high partitioning performance which is promising for effectively separation of the histidine-tagged proteins.
[Mh] Termos MeSH primário: Proteínas Fúngicas/isolamento & purificação
Micelas
Nucleotidases/isolamento & purificação
Leveduras/enzimologia
[Mh] Termos MeSH secundário: Cromatografia Líquida de Alta Pressão
Óxido de Etileno
Proteínas Fúngicas/análise
Extração Líquido-Líquido
Espectrometria de Massas
Nucleotidases/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Micelles); EC 3.1.3.- (Nucleotidases); JJH7GNN18P (Ethylene Oxide)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170620
[St] Status:MEDLINE


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[PMID]:28587841
[Au] Autor:Freitas-Mesquita AL; Meyer-Fernandes JR
[Ad] Endereço:Instituto de Bioquímica Médica Leopoldo de Meis, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, 21941-590, Brazil. Electronic address: anitaleocadio2@gmail.com.
[Ti] Título:3'nucleotidase/nuclease in protozoan parasites: Molecular and biochemical properties and physiological roles.
[So] Source:Exp Parasitol;179:1-6, 2017 Aug.
[Is] ISSN:1090-2449
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:3'-nucleotidase/nuclease (3'NT/NU) is a bi-functional enzyme that is able to hydrolyze 3'-monophosphorylated nucleotides and nucleic acids. This review summarizes the major molecular and biochemical properties of this enzyme in different trypanosomatid species. Sequence analysis of the gene encoding 3'NT/NU in Leishmania and Crithidia species showed that the protein possesses five highly conserved regions that are characteristic of members of the class I nuclease family. 3'NT/NU presents a molecular weight of approximately 40 kDa, which is conserved among the studied species. Throughout the review, we discuss inhibitors and substrate specificity, relating them to the putative structure of the enzyme. Finally, we present the major biological roles performed by 3'NT/NU. The involvement of 3'NT/NU in the purine salvage pathway was confirmed by the increase of activity and expression of the enzyme when the parasites were submitted to purine starvation. The generation of extracellular adenosine is also important to the modulation of the host immune response. Interaction assays involving Leishmania parasites and macrophages indicated that 3'-nucleotidase activity increases the association index between them. Recently, it was shown that 3'NT/NU plays a role in parasite escape from neutrophil extracellular traps, one of the first mechanisms of the host immune system for preventing infection.
[Mh] Termos MeSH primário: Nucleotidases/metabolismo
Trypanosomatina/enzimologia
[Mh] Termos MeSH secundário: Interações Hospedeiro-Parasita
Concentração de Íons de Hidrogênio
Macrófagos/parasitologia
Nucleotidases/antagonistas & inibidores
Nucleotidases/química
Nucleotidases/genética
Especificidade por Substrato
Trypanosomatina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 3.1.3.- (Nucleotidases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170608
[St] Status:MEDLINE


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[PMID]:28266315
[Au] Autor:Liu H; Chen L; Si W; Wang C; Zhu F; Li G; Liu S
[Ad] Endereço:State Key Laboratory of Veterinary Biotechnology, Division of Bacterial Disease of Harbin Veterinary Research Institute, Chinese Academy of Agricultural Science, Harbin, China; Tianjin Key Laboratory of Molecular Drug Research, Tianjin International Joint Academy of Biomedicine, Tianjin, China; Nort
[Ti] Título:Physiology and pathogenicity of cpdB deleted mutant of avian pathogenic Escherichia coli.
[So] Source:Res Vet Sci;111:21-25, 2017 Apr.
[Is] ISSN:1532-2661
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Avian colibacillosis is one of the most common infectious diseases caused partially or entirely by avian pathogenic Escherichia coli (APEC) in birds. In addition to spontaneous infection, APEC can also cause secondary infections that result in greater severity of illness and greater losses to the poultry industry. In order to assess the role of 2', 3'-cyclic phosphodiesterase (cpdB) in APEC on disease physiology and pathogenicity, an avian pathogenic Escherichia coli-34 (APEC-34) cpdB mutant was obtained using the Red system. The cpdB mutant grew at a slower rate than the natural strain APEC-34. Scanning electron microscopy (SEM) indicated that the bacteria of the cpdB mutant were significantly longer than the bacteria observed in the natural strain (P<0.01), and that the width of the cpdB mutant was significantly smaller than its natural counterpart (P<0.01). In order to evaluate the role of cpdB in APEC in the colonization of internal organs (lung, liver and spleen) in poultry, seven-day-old SPF chicks were infected with 10 CFU/chick of the cpdB mutant or the natural strain. No colonizations of cpdB mutants were observed in the internal organs 10days following the infection, though numerous natural strains were observed at 20days following infection. Additionally, the relative expression of division protein ftsZ, outer membrane protein A ompA, ferric uptake regulator fur and tryptophanase tnaA genes in the mutant strain were all significantly lower than in the natural strain (P<0.05 or P<0.01). These results suggested that cpdB is involved in the long-term colonization of APEC in the internal organs of the test subjects. The deletion of the cpdB gene also significantly affected the APEC growth and morphology.
[Mh] Termos MeSH primário: Galinhas/microbiologia
Infecções por Escherichia coli/veterinária
Proteínas de Escherichia coli/genética
Escherichia coli/genética
Nucleotidases/metabolismo
Doenças das Aves Domésticas/microbiologia
[Mh] Termos MeSH secundário: Animais
Escherichia coli/patogenicidade
Escherichia coli/fisiologia
Infecções por Escherichia coli/microbiologia
Deleção de Genes
Regulação Bacteriana da Expressão Gênica/fisiologia
Regulação Enzimológica da Expressão Gênica/fisiologia
Nucleotidases/genética
Virulência
Fatores de Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Virulence Factors); EC 3.1.3.- (Nucleotidases); EC 3.1.3.6 (3'-nucleotidase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170705
[Lr] Data última revisão:
170705
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170308
[St] Status:MEDLINE


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[PMID]:28242355
[Au] Autor:Fracasso M; Da Silva AS; Baldissera MD; Bottari NB; Gabriel ME; Piva MM; Stedille FA; Christ R; Rhoden LA; Henker LC; Moresch VM; Schetinger MR; Mendes RE
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Universidade Federal de Santa Maria, Santa Maria, RS, Brazil; Department of Microbiology and Parasitology, Universidade Federal de Santa Maria, Santa Maria, RS, Brazil.
[Ti] Título:Activities of ectonucleotidases and adenosine deaminase in platelets of cattle experimentally infected by Fasciola hepatica.
[So] Source:Exp Parasitol;176:16-20, 2017 May.
[Is] ISSN:1090-2449
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The enzymatic activities of NTPDase, 5'-nucleotidase and adenosine deaminase (ADA) are important in regulating the concentration of adenine nucleotides, molecules known to be involved on platelet aggregation. Fasciolosis causes coagulation disorders that have not been completely elucidated. Taking into consideration the association between the purinergic system and hemostasis, this study aimed to evaluate the enzymatic activities of NTPDase (hydrolyze ATP and ADP), 5'-nucleotidase (hydrolyze AMP) and ADA (deamination of adenosine) in platelets from cattle experimentally infected by Fasciola hepatica on days 20, 40, 60 and 80 post-infection (PI). For this study, 10 healthy Friesian steers were separated into two groups: the group A (n = 5) was used as uninfected control, and the group B was composed of steers experimentally infected by F. hepatica (n = 5). The number of platelets did not differ between groups in the periods evaluated. Reduction of NTPDase (p < 0.05) hydrolysing ATP (days 20, 40 and 60 PI), and ADP (days 40, 60 and 80 PI), and on 5'-nucleotidase hydrolyzing AMP (days 40 and 60 PI) was observed. A reduction (p < 0.05) in ADA activity on day 20 PI, as well as an increase (p < 0.05) in ADA activity on days 40 and 60 PI was observed when compared to the control. Based on these results, we can conclude that ATP, ADP and AMP hydrolysis and adenosine deamination were altered in platelets of cattle infected by F. hepatica. Considering the importance of the purinergic system in hemostasis, it is believed that those changes may contribute to the coagulation impairment observed in acute fasciolosis described in the literature.
[Mh] Termos MeSH primário: Adenosina Desaminase/sangue
Plaquetas/enzimologia
Doenças dos Bovinos/parasitologia
Fasciolíase/veterinária
Nucleotidases/sangue
[Mh] Termos MeSH secundário: Animais
Bovinos
Doenças dos Bovinos/sangue
Doenças dos Bovinos/enzimologia
Fasciola hepatica/fisiologia
Fasciolíase/sangue
Fasciolíase/enzimologia
Fezes/parasitologia
Fígado/parasitologia
Fígado/patologia
Masculino
Contagem de Ovos de Parasitas/veterinária
Contagem de Plaquetas/veterinária
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.1.3.- (Nucleotidases); EC 3.5.4.4 (Adenosine Deaminase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170411
[Lr] Data última revisão:
170411
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170301
[St] Status:MEDLINE


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[PMID]:27387517
[Au] Autor:Chen L; Wang M; Hou J; Fu J; Shen Y; Liu F; Zhang Z; Bao X
[Ad] Endereço:State Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, China.
[Ti] Título:HAL2 overexpression induces iron acquisition in bdf1Δ cells and enhances their salt resistance.
[So] Source:Curr Genet;63(2):229-239, 2017 May.
[Is] ISSN:1432-0983
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The yeast Saccharomyces cerevisiae is capable of responding to various environmental stresses, such as salt stress. Such responses require a complex network and adjustment of the gene expression network. The goal of this study is to further understand the molecular mechanism of salt stress response in yeast, especially the molecular mechanism related to genes BDF1 and HAL2. The Bromodomain Factor 1 (Bdf1p) is a transcriptional regulator, which is part of the basal transcription factor TFIID. Cells lacking Bdf1p are salt sensitive with an abnormal mitochondrial function. We previously reported that the overexpression of HAL2 or deletion of HDA1 lowers the salt sensitivity of bdf1Δ. To better understand the mechanism behind the HAL2-related response to salt stress, we compared three global transcriptional profiles (bdf1Δ vs WT, bdf1Δ + HAL2 vs bdf1Δ, and bdf1Δhda1Δ vs bdf1Δ) in response to salt stress using DNA microarrays. Our results reveal that genes for iron acquisition and cellular and mitochondrial remodeling are induced by HAL2. Overexpression of HAL2 decreases the concentration of nitric oxide. Mitochondrial iron-sulfur cluster (ISC) assembly also decreases in bdf1Δ + HAL2. These changes are similar to the changes of transcriptional profiles induced by iron starvation. Taken together, our data suggest that mitochondrial functions and iron homeostasis play an important role in bdf1Δ-induced salt sensitivity and salt stress response in yeast.
[Mh] Termos MeSH primário: Regulação Fúngica da Expressão Gênica/genética
Ferro/metabolismo
Nucleotidases/genética
Proteínas de Saccharomyces cerevisiae/genética
Tolerância a Sal/genética
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Perfilação da Expressão Gênica/métodos
Regulação Fúngica da Expressão Gênica/efeitos dos fármacos
Ontologia Genética
Immunoblotting
Mutação
Nucleotidases/metabolismo
Análise de Sequência com Séries de Oligonucleotídeos
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Transdução de Sinais/genética
Cloreto de Sódio/farmacologia
Estresse Fisiológico
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BDF1 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factors); 451W47IQ8X (Sodium Chloride); E1UOL152H7 (Iron); EC 3.1.3.- (Nucleotidases); EC 3.1.3.7 (bisphosphoadenylate 3'-nucleotidase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160709
[St] Status:MEDLINE
[do] DOI:10.1007/s00294-016-0628-9


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[PMID]:27784292
[Au] Autor:Terakawa A; Natsume A; Okada A; Nishihata S; Kuse J; Tanaka K; Takenaka S; Ishikawa S; Yoshida KI
[Ad] Endereço:Department of Agrobioscience, Kobe University, 1-1 Rokkodai, Nada, Kobe, Hyogo, 657-8501, Japan.
[Ti] Título:Bacillus subtilis 5'-nucleotidases with various functions and substrate specificities.
[So] Source:BMC Microbiol;16(1):249, 2016 Oct 26.
[Is] ISSN:1471-2180
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: In Escherichia coli, nagD, yrfG, yjjG, yieH, yigL, surE, and yfbR encode 5'-nucleotidases that hydrolyze the phosphate group of 5'-nucleotides. In Bacillus subtilis, genes encoding 5'-nucleotidase have remained to be identified. RESULTS: We found that B. subtilis ycsE, araL, yutF, ysaA, and yqeG show suggestive similarities to nagD. Here, we expressed them in E. coli to purify the respective His -tagged proteins. YcsE exhibited significant 5'-nucleotidase activity with a broader specificity, whereas the other four enzymes had rather weak but suggestive activities with various capacities and substrate specificities. In contrast, B. subtilis yktC shares high similarity with E. coli suhB encoding an inositol monophosphatase. YktC exhibited inositol monophosphatase activity as well as 5'-nucleotidase activity preferential for GMP and IMP. The ycsE, yktC, and yqeG genes are induced by oxidative stress and were dispensable, although yqeG was required to maintain normal growth on solid medium. In the presence of diamide, only mutants lacking yktC exhibited enhanced growth defects, whereas the other mutants without ycsE or yqeG did not. CONCLUSIONS: Accordingly, in B. subtilis, at least YcsE and YktC acted as major 5'-nucleotidases and the four minor enzymes might function when the intracellular concentrations of substrates are sufficiently high. In addition, YktC is involved in resistance to oxidative stress caused by diamide, while YqeG is necessary for normal colony formation on solid medium.
[Mh] Termos MeSH primário: 5´-Nucleotidase/metabolismo
Bacillus subtilis/enzimologia
[Mh] Termos MeSH secundário: 5'-Nucleotidase/genética
Motivos de Aminoácidos
Sequência de Aminoácidos
Bacillus subtilis/genética
Ativação Enzimática
Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Genes Bacterianos
Hidrolases/genética
Hidrolases/metabolismo
Fosfatos de Inositol/metabolismo
Nucleotidases/metabolismo
Estresse Oxidativo/genética
Monoéster Fosfórico Hidrolases/genética
Monoéster Fosfórico Hidrolases/metabolismo
Homologia de Sequência
Células-Tronco
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Inositol Phosphates); EC 3.- (Hydrolases); EC 3.1.3.- (NagD protein, E coli); EC 3.1.3.- (Nucleotidases); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.1.3.25 (myo-inositol-1 (or 4)-monophosphatase); EC 3.1.3.5 (5'-Nucleotidase); EC 3.8.1.2 (2-haloacid dehalogenase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170608
[Lr] Data última revisão:
170608
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161028
[St] Status:MEDLINE



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