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Pesquisa : D08.811.682.662.582 [Categoria DeCS]
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[PMID]:28619819
[Au] Autor:Huang J; Reilein A; Kalderon D
[Ad] Endereço:State Key Laboratory of Rice Biology, Institute of Insect Sciences, Zhejiang University, Hangzhou, 310058, China.
[Ti] Título:Yorkie and Hedgehog independently restrict BMP production in escort cells to permit germline differentiation in the ovary.
[So] Source:Development;144(14):2584-2594, 2017 07 15.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Multiple signaling pathways guide the behavior and differentiation of both germline stem cells (GSCs) and somatic follicle stem cells (FSCs) in the germarium, necessitating careful control of signal generation, range and responses. Signal integration involves escort cells (ECs), which promote differentiation of the GSC derivatives they envelop, provide niche signals for FSCs and derive directly from FSCs in adults. Hedgehog (Hh) signaling induces the Hippo pathway effector Yorkie (Yki) to promote proliferation and maintenance of FSCs, but Hh also signals to ECs, which are quiescent. Here, we show that in ECs both Hh and Yki limit production of BMP ligands to allow germline differentiation. Loss of Yki produced a more severe germarial phenotype than loss of Hh signaling and principally induced a different BMP ligand. Moreover, Yki activity reporters and epistasis tests showed that Yki does not mediate the key actions of Hh signaling in ECs. Thus, both the coupling and output of the Hh and Yki signaling pathways differ between FSCs and ECs despite their proximity and the fact that FSCs give rise directly to ECs.
[Mh] Termos MeSH primário: Proteínas Morfogenéticas Ósseas/biossíntese
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/citologia
Drosophila melanogaster/metabolismo
Proteínas Hedgehog/metabolismo
Proteínas Nucleares/metabolismo
Ovário/citologia
Ovário/metabolismo
Transativadores/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Diferenciação Celular/genética
Diferenciação Celular/fisiologia
Proteínas de Drosophila/deficiência
Proteínas de Drosophila/genética
Drosophila melanogaster/genética
Feminino
Genes de Insetos
Proteínas Hedgehog/genética
Proteínas Nucleares/genética
Oogênese/genética
Oogênese/fisiologia
Oxirredutases N-Desmetilantes/genética
Oxirredutases N-Desmetilantes/metabolismo
Transdução de Sinais
Receptor Smoothened/genética
Receptor Smoothened/metabolismo
Nicho de Células-Tronco
Células-Tronco/citologia
Células-Tronco/metabolismo
Transativadores/genética
Fator de Crescimento Transformador beta/deficiência
Fator de Crescimento Transformador beta/genética
Fator de Crescimento Transformador beta/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Bone Morphogenetic Proteins); 0 (Drosophila Proteins); 0 (Hedgehog Proteins); 0 (Nuclear Proteins); 0 (Smoothened Receptor); 0 (Trans-Activators); 0 (Transforming Growth Factor beta); 0 (Yorkie protein, Drosophila); 0 (dpp protein, Drosophila); 0 (gbb protein, Drosophila); 0 (smoothened protein, Drosophila); 149291-21-4 (hedgehog protein, Drosophila); EC 1.5.- (Lsd1 protein, Drosophila); EC 1.5.- (Oxidoreductases, N-Demethylating)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170617
[St] Status:MEDLINE
[do] DOI:10.1242/dev.147702


  2 / 3406 MEDLINE  
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[PMID]:28515319
[Au] Autor:Ulfig A; Fröbel J; Lausberg F; Blümmel AS; Heide AK; Müller M; Freudl R
[Ad] Endereço:From the Institute of Bio- and Geosciences, IBG-1: Biotechnology, Forschungszentrum Jülich GmbH, Wilhelm-Johnen-Strasse, D-52425 Jülich, Germany and.
[Ti] Título:The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex.
[So] Source:J Biol Chem;292(26):10865-10882, 2017 Jun 30.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The twin-arginine translocation (Tat) pathway transports folded proteins across bacterial membranes. Tat precursor proteins possess a conserved twin-arginine (RR) motif in their signal peptides that is involved in their binding to the Tat translocase, but some facets of this interaction remain unclear. Here, we investigated the role of the hydrophobic (h-) region of the trimethylamine -oxide reductase (TorA) signal peptide in TatBC receptor binding and We show that besides the RR motif, a minimal, functional h-region in the signal peptide is required for Tat-dependent export in Furthermore, we identified mutations in the h-region that synergistically suppressed the export defect of a TorA[KQ]-30aa-MalE Tat reporter protein in which the RR motif was replaced with a lysine-glutamine pair. Strikingly, all suppressor mutations increased the hydrophobicity of the h-region. By systematically replacing a neutral residue in the h-region with various amino acids, we detected a positive correlation between the hydrophobicity of the h-region and the translocation efficiency of the resulting reporter variants. cross-linking of residues located in the periplasmically-oriented part of the TatBC receptor to TorA[KQ]-30aa-MalE reporter variants harboring a more hydrophobic h-region in their signal peptides confirmed that unlike in TorA[KQ]-30aa-MalE with an unaltered h-region, the mutated reporters moved deep into the TatBC-binding cavity. Our results clearly indicate that, besides the Tat motif, the h-region of the Tat signal peptides is another important binding determinant that significantly contributes to the productive interaction of Tat precursor proteins with the TatBC receptor complex.
[Mh] Termos MeSH primário: Precursores Enzimáticos/metabolismo
Proteínas de Escherichia coli/metabolismo
Escherichia coli/metabolismo
Proteínas de Membrana Transportadoras/metabolismo
Oxirredutases N-Desmetilantes/metabolismo
Sinais Direcionadores de Proteínas/fisiologia
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Precursores Enzimáticos/genética
Escherichia coli/genética
Proteínas de Escherichia coli/genética
Proteínas de Membrana Transportadoras/genética
Oxirredutases N-Desmetilantes/genética
Periplasma/genética
Periplasma/metabolismo
Domínios Proteicos
Transporte Proteico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Precursors); 0 (Escherichia coli Proteins); 0 (Membrane Transport Proteins); 0 (Protein Sorting Signals); 0 (TatB protein, E coli); 0 (TatC protein, E coli); EC 1.5.- (Oxidoreductases, N-Demethylating); EC 1.5.8.2 (trimethylamine dehydrogenase)
[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:170519
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.788950


  3 / 3406 MEDLINE  
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[PMID]:28496033
[Au] Autor:Ding L; Zang L; Zhang Y; Zhang Y; Wang X; Ai W; Ding N; Wang H
[Ad] Endereço:School of Physical Education and Sport Sciences, Wenzhou Medical University, China.
[Ti] Título:Joint toxicity of fluoroquinolone and tetracycline antibiotics to zebrafish (Danio rerio) based on biochemical biomarkers and histopathological observation.
[So] Source:J Toxicol Sci;42(3):267-280, 2017.
[Is] ISSN:1880-3989
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Herein, we report on the joint toxicity of four fluoroquinolones and two tetracyclines (ß-diketone antibiotics-DKAs) to zebrafish based on a series of toxicological endpoints and histopathological observations. A positive dose-dependence was observed in DKA-exposure groups with a 72-hpf EC of 130.3 mg/L for hatching rate, 120-hpf LC of 149.8 mg/L, and 120-hpf EC of 135.1 mg/L for malformation rate. When zebrafish at 60 dpf were exposed to a series of DKA concentrations (45, 60 and 90 mg/L) for 7, 14 and 21 days, creatine kinase and AChE activities were significantly induced, and intracellular malondialdehyde increased in all treatments except for the 45 mg/L treatment. The transcription levels of AHRRa from livers were significantly (p < 0.05) up-regulated in all treatments after two months of DKA exposure. CKma expression from skeletal muscle was significantly down-regulated in the 90 mg/L treatment. A remarkable down-regulation of CYP3A65 was observed in the 60 mg/L treatment. DKA exposure resulted in severe tissue damage including mitochondria swelling, reduction of mitochondrial cristae, deepening of mitochondrial cristae bands, and decreasing and even disappearance of the rough endoplasmic reticulum. Total sperm motility was decreased by ca. 30% due to DKA exposure. These results provide important information for toxicity and health risks due to mixed DKA exposure in aquatic environments.
[Mh] Termos MeSH primário: Acetilcolinesterase/metabolismo
Antibacterianos/toxicidade
Hidrocarboneto de Aril Hidroxilases/genética
Hidrocarboneto de Aril Hidroxilases/metabolismo
Creatina Quinase/metabolismo
Fluoroquinolonas/toxicidade
Expressão Gênica/efeitos dos fármacos
Malondialdeído/metabolismo
Oxirredutases N-Desmetilantes/genética
Oxirredutases N-Desmetilantes/metabolismo
Motilidade Espermática/efeitos dos fármacos
Tetraciclinas/toxicidade
Proteínas de Peixe-Zebra/genética
Proteínas de Peixe-Zebra/metabolismo
[Mh] Termos MeSH secundário: Animais
Relação Dose-Resposta a Droga
Regulação para Baixo/efeitos dos fármacos
Retículo Endoplasmático Rugoso/efeitos dos fármacos
Fígado/metabolismo
Mitocôndrias/efeitos dos fármacos
Dilatação Mitocondrial/efeitos dos fármacos
Proteínas Repressoras/genética
Reprodução/efeitos dos fármacos
Transcrição Genética/efeitos dos fármacos
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Fluoroquinolones); 0 (Repressor Proteins); 0 (Tetracyclines); 0 (Zebrafish Proteins); 0 (aryl hydrocarbon receptor repressor 1, Danio rerio); 4Y8F71G49Q (Malondialdehyde); EC 1.14.14.1 (Aryl Hydrocarbon Hydroxylases); EC 1.14.14.1 (cytochrome P-450 CYP3A65, zebrafish); EC 1.5.- (Oxidoreductases, N-Demethylating); EC 2.7.3.2 (Creatine Kinase); EC 3.1.1.7 (Acetylcholinesterase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170513
[St] Status:MEDLINE
[do] DOI:10.2131/jts.42.267


  4 / 3406 MEDLINE  
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[PMID]:28406950
[Au] Autor:Kim J; Kim MK; Jung S; Lim JE; Shin MH; Kim YJ; Oh B
[Ad] Endereço:Department of Preventive Medicine, College of Medicine, Hanyang University, Seoul, South Korea.
[Ti] Título:Interaction of iron status with single nucleotide polymorphisms on incidence of type 2 diabetes.
[So] Source:PLoS One;12(4):e0175681, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The objective of this study is to find single nucleotide polymorphisms (SNPs) associated with a risk of Type 2 diabetes (T2D) in Korean adults and to investigate the longitudinal association between these SNPs and T2D and the interaction effects of iron intake and average hemoglobin level. Data from the KoGES_Ansan and Ansung Study were used. Gene-iron interaction analysis was conducted using a two-step approach. To select candidate SNPs associated with T2D, a total of 7,935 adults at baseline were included in genome-wide association analysis (step one). After excluding T2D prevalent cases, prospective analyses were conducted with 7,024 adults aged 40-69 (step two). The association of selected SNPs and iron status with T2D and their interaction were determined using a Cox proportional hazard model. A total of 3 SNPs [rs9465871 (CDKAL1), rs10761745 (JMJD1C), and rs163177 (KCNQ1)] were selected as candidate SNPs related to T2D. Among them, rs10761745 (JMJD1C) and rs163177 (KCNQ1) were prospectively associated with T2D. High iron intake was also prospectively associated with the risk of T2D after adjusting for covariates. Average hemoglobin level was positively associated with T2D after adjusting for covariates in women. We also found significant interaction effects between rs10761745 (JMJD1C) and average hemoglobin levels on the risk of T2D among women with normal inflammation and without anemia at baseline. In conclusion, KCNQ1 and JMJD1C may prospectively contribute to the risk of T2D incidence among adults over the age of 40 and JMJD1C, but CDKAL1 may not, and iron status may interactively contribute to T2D incidence in women.
[Mh] Termos MeSH primário: Diabetes Mellitus Tipo 2/epidemiologia
Ferro/metabolismo
Histona Desmetilases com o Domínio Jumonji/genética
Canal de Potássio KCNQ1/genética
Oxirredutases N-Desmetilantes/genética
Polimorfismo de Nucleotídeo Único
tRNA Metiltransferases/genética
[Mh] Termos MeSH secundário: Adulto
Fatores Etários
Idoso
Grupo com Ancestrais do Continente Asiático/genética
Diabetes Mellitus Tipo 2/genética
Diabetes Mellitus Tipo 2/metabolismo
Feminino
Predisposição Genética para Doença
Estudo de Associação Genômica Ampla
Hemoglobinas/metabolismo
Seres Humanos
Incidência
Masculino
Meia-Idade
Estudos Prospectivos
República da Coreia/epidemiologia
Fatores Sexuais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hemoglobins); 0 (KCNQ1 Potassium Channel); 0 (KCNQ1 protein, human); E1UOL152H7 (Iron); EC 1.14.11.- (JMJD1C protein, human); EC 1.14.11.- (Jumonji Domain-Containing Histone Demethylases); EC 1.5.- (Oxidoreductases, N-Demethylating); EC 2.1.1.- (tRNA Methyltransferases); EC 2.8.4.5 (CDKAL1 protein, human)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170504
[Lr] Data última revisão:
170504
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175681


  5 / 3406 MEDLINE  
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[PMID]:28010187
[Au] Autor:Klink VP; Sharma K; Pant SR; McNeece B; Niraula P; Lawrence GW
[Ad] Endereço:a Department of Biological Sciences , Mississippi State University , Mississippi State , MS , USA.
[Ti] Título:Components of the SNARE-containing regulon are co-regulated in root cells undergoing defense.
[So] Source:Plant Signal Behav;12(2):e1274481, 2017 Feb.
[Is] ISSN:1559-2324
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The term regulon has been coined in the genetic model plant Arabidopsis thaliana, denoting a structural and physiological defense apparatus defined genetically through the identification of the penetration (pen) mutants. The regulon is composed partially by the soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) syntaxin PEN1. PEN1 has homology to a Saccharomyces cerevisae gene that regulates a Secretion (Sec) protein, Suppressor of Sec 1 (Sso1p). The regulon is also composed of the ß-glucosidase (PEN2) and an ATP binding cassette (ABC) transporter (PEN3). While important in inhibiting pathogen infection, limited observations have been made regarding the transcriptional regulation of regulon genes until now. Experiments made using the model agricultural Glycine max (soybean) have identified co-regulated gene expression of regulon components. The results explain the observation of hundreds of genes expressed specifically in the root cells undergoing the natural process of defense. Data regarding additional G. max genes functioning within the context of the regulon are presented here, including Sec 14, Sec 4 and Sec 23. Other examined G. max homologs of membrane fusion genes include an endosomal bromo domain-containing protein1 (Bro1), syntaxin6 (SYP6), SYP131, SYP71, SYP8, Bet1, coatomer epsilon (ϵ-COP), a coatomer zeta (ζ-COP) paralog and an ER to Golgi component (ERGIC) protein. Furthermore, the effectiveness of biochemical pathways that would function within the context of the regulon ave been examined, including xyloglucan xylosyltransferase (XXT), reticuline oxidase (RO) and galactinol synthase (GS). The experiments have unveiled the importance of the regulon during defense in the root and show how the deposition of callose relates to the process.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/metabolismo
[Mh] Termos MeSH secundário: Transportadores de Cassetes de Ligação de ATP/genética
Transportadores de Cassetes de Ligação de ATP/metabolismo
Arabidopsis/genética
Proteínas de Arabidopsis/genética
Galactosiltransferases/genética
Galactosiltransferases/metabolismo
Glucanos/metabolismo
N-Glicosil Hidrolases/genética
N-Glicosil Hidrolases/metabolismo
Oxirredutases N-Desmetilantes/genética
Oxirredutases N-Desmetilantes/metabolismo
Pentosiltransferases/genética
Pentosiltransferases/metabolismo
Raízes de Plantas/genética
Raízes de Plantas/metabolismo
Regulon/genética
Proteínas SNARE/genética
Proteínas SNARE/metabolismo
Feijão de Soja/genética
Feijão de Soja/metabolismo
beta-Glucosidase/genética
beta-Glucosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Glucans); 0 (PDR8 protein, Arabidopsis); 0 (SNARE Proteins); 9064-51-1 (callose); EC 1.21.3.3 (reticuline oxidase); EC 1.5.- (Oxidoreductases, N-Demethylating); EC 2.4.1.- (Galactosyltransferases); EC 2.4.1.123 (inositol 1-alpha-galactosyltransferase); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.- (xyloglucan xylosyltransferase); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.2.- (N-Glycosyl Hydrolases); EC 3.2.2.- (PEN2 protein, Arabidopsis)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161225
[St] Status:MEDLINE
[do] DOI:10.1080/15592324.2016.1274481


  6 / 3406 MEDLINE  
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[PMID]:27984091
[Au] Autor:Frain KM; Jones AS; Schoner R; Walker KL; Robinson C
[Ad] Endereço:School of Biosciences, University of Kent, Canterbury CT2 7NJ, United Kingdom.
[Ti] Título:The Bacillus subtilis TatAdCd system exhibits an extreme level of substrate selectivity.
[So] Source:Biochim Biophys Acta;1864(1):202-208, 2017 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The Tat system preferentially transports correctly folded proteins across the bacterial membrane although little is known of the proofreading mechanism. Most research has focused on TatABC systems from Gram-negative bacteria, especially Escherichia coli, and much less is known of the TatAC-type systems from Gram-positive organisms. We have previously shown that the Bacillus subtilis TatAdCd system is functional in an E. coli tat null background and able to transport TorA-GFP and native TorA (TMAO reductase); here, we examined its ability to transport other proteins bearing a TorA signal sequence. We show that whereas E. coli TatABC transports a wide range of biotherapeutics including human growth hormone, interferon α2b, a VH domain protein and 2 different scFvs, TatAdCd transports the scFvs but completely rejects the other proteins. The system also rejects two native E. coli substrates, NrfC and FhuD. Moreover, we have shown that TatABC will transport a wide range of folded scFv variants with the surface altered to incorporate multiple salt bridges, charged residues (5 glutamate, lysine or arginine), or hydrophobic residues (up to 6 leucines). In contrast, TatAdCd completely rejects many of these variants including those with 5 or 6 added Leu residues. The combined data show that the TatABC and TatAdCd systems have very different substrate selectivities, with the TatAdCd system displaying an extreme level of selectivity when compared to the E. coli system. The data also provide a preliminary suggestion that TatAdCd may not tolerate substrates that contain surface domains with a level of hydrophobicity above a certain threshold.
[Mh] Termos MeSH primário: Bacillus subtilis/metabolismo
Proteínas de Escherichia coli/metabolismo
Proteínas de Membrana Transportadoras/metabolismo
Oxirredutases N-Desmetilantes/metabolismo
Anticorpos de Cadeia Única/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Bacillus subtilis/genética
Transporte Biológico
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas de Escherichia coli/genética
Expressão Gênica
Genes Reporter
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Hormônio do Crescimento Humano/química
Hormônio do Crescimento Humano/metabolismo
Interações Hidrofóbicas e Hidrofílicas
Interferon-alfa/química
Interferon-alfa/metabolismo
Proteínas de Membrana Transportadoras/genética
Oxirredutases N-Desmetilantes/genética
Dobramento de Proteína
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Anticorpos de Cadeia Única/química
Anticorpos de Domínio Único/química
Anticorpos de Domínio Único/metabolismo
Eletricidade Estática
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Interferon-alpha); 0 (Interferon-alpha2b); 0 (Membrane Transport Proteins); 0 (Recombinant Fusion Proteins); 0 (Single-Chain Antibodies); 0 (Single-Domain Antibodies); 0 (twin-arginine translocase complex, E coli); 12629-01-5 (Human Growth Hormone); 147336-22-9 (Green Fluorescent Proteins); EC 1.5.- (Oxidoreductases, N-Demethylating); EC 1.5.8.2 (trimethylamine dehydrogenase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161217
[St] Status:MEDLINE


  7 / 3406 MEDLINE  
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[PMID]:27940577
[Au] Autor:Costa KC; Glasser NR; Conway SJ; Newman DK
[Ad] Endereço:Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
[Ti] Título:Pyocyanin degradation by a tautomerizing demethylase inhibits Pseudomonas aeruginosa biofilms.
[So] Source:Science;355(6321):170-173, 2017 01 13.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The opportunistic pathogen Pseudomonas aeruginosa produces colorful redox-active metabolites called phenazines, which underpin biofilm development, virulence, and clinical outcomes. Although phenazines exist in many forms, the best studied is pyocyanin. Here, we describe pyocyanin demethylase (PodA), a hitherto uncharacterized protein that oxidizes the pyocyanin methyl group to formaldehyde and reduces the pyrazine ring via an unusual tautomerizing demethylation reaction. Treatment with PodA disrupts P. aeruginosa biofilm formation similarly to DNase, suggesting interference with the pyocyanin-dependent release of extracellular DNA into the matrix. PodA-dependent pyocyanin demethylation also restricts established biofilm aggregate populations experiencing anoxic conditions. Together, these results show that modulating extracellular redox-active metabolites can influence the fitness of a biofilm-forming microorganism.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Bactérias/farmacologia
Biofilmes/efeitos dos fármacos
Mycobacterium fortuitum/enzimologia
Oxirredutases N-Desmetilantes/química
Oxirredutases N-Desmetilantes/farmacologia
Pseudomonas aeruginosa/efeitos dos fármacos
Piocianina/química
[Mh] Termos MeSH secundário: Cristalografia por Raios X
DNA/química
Metilação
Oxirredução
Pseudomonas aeruginosa/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Bacterial Proteins); 9007-49-2 (DNA); 9OQM399341 (Pyocyanine); EC 1.5.- (Oxidoreductases, N-Demethylating)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE
[do] DOI:10.1126/science.aag3180


  8 / 3406 MEDLINE  
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[PMID]:27851736
[Au] Autor:Ortmayer M; Lafite P; Menon BR; Tralau T; Fisher K; Denkhaus L; Scrutton NS; Rigby SE; Munro AW; Hay S; Leys D
[Ad] Endereço:Manchester Institute of Biotechnology, School of Chemistry, 131 Princess Street, University of Manchester, Manchester M1 7DN, UK.
[Ti] Título:An oxidative N-demethylase reveals PAS transition from ubiquitous sensor to enzyme.
[So] Source:Nature;539(7630):593-597, 2016 11 24.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The universal Per-ARNT-Sim (PAS) domain functions as a signal transduction module involved in sensing diverse stimuli such as small molecules, light, redox state and gases. The highly evolvable PAS scaffold can bind a broad range of ligands, including haem, flavins and metal ions. However, although these ligands can support catalytic activity, to our knowledge no enzymatic PAS domain has been found. Here we report characterization of the first PAS enzyme: a haem-dependent oxidative N-demethylase. Unrelated to other amine oxidases, this enzyme contains haem, flavin mononucleotide, 2Fe-2S and tetrahydrofolic acid cofactors, and specifically catalyses the NADPH-dependent oxidation of dimethylamine. The structure of the α subunit reveals that it is a haem-binding PAS domain, similar in structure to PAS gas sensors. The dimethylamine substrate forms part of a highly polarized oxygen-binding site, and directly assists oxygen activation by acting as both an electron and proton donor. Our data reveal that the ubiquitous PAS domain can make the transition from sensor to enzyme, suggesting that the PAS scaffold can support the development of artificial enzymes.
[Mh] Termos MeSH primário: Oxirredutases N-Desmetilantes/química
Oxirredutases N-Desmetilantes/metabolismo
Pseudomonas mendocina/enzimologia
[Mh] Termos MeSH secundário: Sítios de Ligação
Coenzimas/metabolismo
Cristalografia por Raios X
Dimetilaminas/metabolismo
Mononucleotídeo de Flavina/metabolismo
Heme/metabolismo
Proteínas com Ferro-Enxofre/química
Proteínas com Ferro-Enxofre/metabolismo
Modelos Moleculares
NADP/metabolismo
Oxirredução
Oxigênio/metabolismo
Domínios Proteicos
Subunidades Proteicas/química
Subunidades Proteicas/metabolismo
Tetra-Hidrofolatos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Coenzymes); 0 (Dimethylamines); 0 (Iron-Sulfur Proteins); 0 (Protein Subunits); 0 (Tetrahydrofolates); 42VZT0U6YR (Heme); 43ZWB253H4 (5,6,7,8-tetrahydrofolic acid); 53-59-8 (NADP); 7N464URE7E (Flavin Mononucleotide); ARQ8157E0Q (dimethylamine); EC 1.5.- (Oxidoreductases, N-Demethylating); S88TT14065 (Oxygen)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161117
[St] Status:MEDLINE
[do] DOI:10.1038/nature20159


  9 / 3406 MEDLINE  
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[PMID]:27612494
[Au] Autor:Harel A; Häggblom MM; Falkowski PG; Yee N
[Ad] Endereço:Department of Vegetable Research, Institute of Plant Sciences, Volcani Center, ARO, 68 HaMaccabim Road, Rishon LeZion 7505101, ISRAEL Environmental Biophysics and Molecular Ecology Program, Department of Marine and Coastal Science, Rutgers the State University of New Jersey, 71 Dudley Road, New Brun
[Ti] Título:Evolution of prokaryotic respiratory molybdoenzymes and the frequency of their genomic co-occurrence.
[So] Source:FEMS Microbiol Ecol;92(12), 2016 Dec.
[Is] ISSN:1574-6941
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Molybdoenzymes are an ancient protein family found in phylogenetically and ecologically diverse prokaryotes. Under anaerobic conditions, respiratory molybdoenzymes catalyze redox reactions that transfer electrons to a variety of substrates that act as terminal electron acceptors for energy generation. Here, we used probe sequences to conduct an extensive genomic survey and phylogenetic inference for NarG, DmsA, TorA and nine other respiratory molybdoenzyme subfamilies. Our analysis demonstrates their abundance in 60% of prokaryotic phyla. In contrast to many other autonomic genetic units in prokaryotes, the major route of evolution of their predominant subfamilies is vertical gene transfer, gene duplication and divergence. Our results show the robustness of genomic co-occurrence of respiratory molybdoenzymes genes, found in the majority of studied species, for most of the enzyme subfamilies. Genomes which encode for multiple respiratory molybdoenzymes are also enriched in genes regulating replication, recombination and mobility of genetic elements. Respiratory molybdoenzymes were found in prokaryotes associated with diverse environments occupying terrestrial, aquatic, food and host-related habitats, emphasizing their essential role in adaptation of prokaryotes to changing environments. Interestingly, host-associated prokaryotes such as human pathogens more frequently carry multiple respiratory molybdoenzyme genes compared with non-host-associated prokaryotes, highlighting the importance of metabolic flexibility in host-microbiome environments.
[Mh] Termos MeSH primário: Archaea/enzimologia
Bactérias/enzimologia
Evolução Biológica
Genoma Arqueal/genética
Genoma Bacteriano/genética
Nitrato Redutase/genética
Oxirredutases N-Desmetilantes/genética
[Mh] Termos MeSH secundário: Archaea/genética
Archaea/metabolismo
Bactérias/genética
Bactérias/metabolismo
Genômica
Seres Humanos
Microbiota/genética
Molibdênio/química
Oxirredução
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
81AH48963U (Molybdenum); EC 1.5.- (Oxidoreductases, N-Demethylating); EC 1.5.8.2 (trimethylamine dehydrogenase); EC 1.7.99.4 (Nitrate Reductase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170803
[Lr] Data última revisão:
170803
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160911
[St] Status:MEDLINE


  10 / 3406 MEDLINE  
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[PMID]:27596288
[Au] Autor:Liedschulte V; Schwaar JD; Laparra H; Vuarnoz A; Philippon B; Bakaher N; Sierro N; Bovet L; Lang G; Goepfert S
[Ad] Endereço:PMI R&D, Philip Morris Products SA, (part of Philip Morris International Group of Companies), Neuchâtel, Switzerland. Electronic address: Verena.Liedschulte@pmi.com.
[Ti] Título:Identification of CYP82E21 as a functional nicotine N-demethylase in tobacco flowers.
[So] Source:Phytochemistry;131:9-16, 2016 Nov.
[Is] ISSN:1873-3700
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In the tobacco plant, nicotine N-demethylase enzymes (NND) belonging to the cytochrome P450 family catalyse the conversion of nicotine to nornicotine, the precursor of the carcinogenic tobacco-specific N-nitrosamine, N-nitrosonornicotine. To date three demethylase genes, namely CYP82E4, CYP82E5 and CYP82E10, have been shown to be involved in this process, while the related CYP82E2 and CYP82E3 genes are not functional. We have identified a further gene named CYP82E21 encoding a putative nicotine N-demethylase closely related to the CYP82E genes. The CYP82E21 gene was found in all Nicotiana tabacum cultivars analysed and originates from the tobacco ancestor Nicotiana tomentosiformis. We show that, in contrast to all other previously characterized NND genes, CYP82E21 is not expressed in green or senescent leaves, but in flowers, more specifically in ovaries. The nicotine N-demethylase activity of CYP82E21 was confirmed by ectopic expression of the coding sequence in a tobacco line lacking functional CYP82E4, CYP82E5 and CYP82E10 genes, resulting in an eightfold increase of nicotine demethylation compared to the control plants. Furthermore, nornicotine formation can be reduced in ovaries by introducing a CYP82E21-specific RNAi construct. Together, our results demonstrate that the CYP82E21 gene encodes a functional ovary-specific nicotine N-demethylase.
[Mh] Termos MeSH primário: Sistema Enzimático do Citocromo P-450/metabolismo
Tabaco/enzimologia
[Mh] Termos MeSH secundário: Sistema Enzimático do Citocromo P-450/genética
Flores/metabolismo
Nicotina/análogos & derivados
Nicotina/biossíntese
Nicotina/metabolismo
Nitrosaminas/metabolismo
Oxirredutases N-Desmetilantes/metabolismo
Folhas de Planta/metabolismo
Proteínas de Plantas/metabolismo
Interferência de RNA/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nitrosamines); 0 (Plant Proteins); 6M3C89ZY6R (Nicotine); 83H6L5QD8Z (nornicotine); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 1.- (nicotine demethylase, tobacco); EC 1.5.- (Oxidoreductases, N-Demethylating); X656TZ86DX (N'-nitrosonornicotine)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170310
[Lr] Data última revisão:
170310
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160907
[St] Status:MEDLINE



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