Base de dados : MEDLINE
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[PMID]:28807600
[Au] Autor:Shin SM; Song SH; Lee JW; Kwak MK; Kang SO
[Ad] Endereço:Laboratory of Biophysics, School of Biological Sciences, and Institute of Microbiology, Seoul National University, Seoul 151-742, Republic of Korea.
[Ti] Título:Methylglyoxal synthase regulates cell elongation via alterations of cellular methylglyoxal and spermidine content in Bacillus subtilis.
[So] Source:Int J Biochem Cell Biol;91(Pt A):14-28, 2017 Oct.
[Is] ISSN:1878-5875
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Methylglyoxal regulates cell division and differentiation through its interaction with polyamines. Loss of their biosynthesizing enzyme causes physiological impairment and cell elongation in eukaryotes. However, the reciprocal effects of methylglyoxal and polyamine production and its regulatory metabolic switches on morphological changes in prokaryotes have not been addressed. Here, Bacillus subtilis methylglyoxal synthase (mgsA) and polyamine biosynthesizing genes encoding arginine decarboxylase (SpeA), agmatinase (SpeB), and spermidine synthase (SpeE), were disrupted or overexpressed. Treatment of 0.2mM methylglyoxal and 1mM spermidine led to the elongation and shortening of B. subtilis wild-type cells to 12.38±3.21µm (P<0.05) and 3.24±0.73µm (P<0.01), respectively, compared to untreated cells (5.72±0.68µm). mgsA-deficient (mgsA ) and -overexpressing (mgsA ) mutants also demonstrated cell shortening and elongation, similar to speB- and speE-deficient (speB and speE ) and -overexpressing (speB and speE ) mutants. Importantly, both mgsA-depleted speB and speE mutants (speB /mgsA and speE /mgsA ) were drastically shortened to 24.5% and 23.8% of parental speB and speE mutants, respectively. These phenotypes were associated with reciprocal alterations of mgsA and polyamine transcripts governed by the contents of methylglyoxal and spermidine, which are involved in enzymatic or genetic metabolite-control mechanisms. Additionally, biophysically detected methylglyoxal-spermidine Schiff bases did not affect morphogenesis. Taken together, the findings indicate that methylglyoxal triggers cell elongation. Furthermore, cells with methylglyoxal accumulation commonly exhibit an elongated rod-shaped morphology through upregulation of mgsA, polyamine genes, and the global regulator spx, as well as repression of the cell division and shape regulator, FtsZ.
[Mh] Termos MeSH primário: Bacillus subtilis/citologia
Bacillus subtilis/enzimologia
Carbono-Oxigênio Liases/metabolismo
Aldeído Pirúvico/metabolismo
Espermidina/metabolismo
[Mh] Termos MeSH secundário: Bacillus subtilis/efeitos dos fármacos
Bacillus subtilis/metabolismo
Carbono-Oxigênio Liases/genética
Aldeído Pirúvico/farmacologia
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Espermidina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 722KLD7415 (Pyruvaldehyde); EC 4.2.- (Carbon-Oxygen Lyases); EC 4.2.3.3 (methylglyoxal synthase); U87FK77H25 (Spermidine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170816
[St] Status:MEDLINE


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[PMID]:28675039
[Au] Autor:Sagong HY; Kim KJ
[Ad] Endereço:KNU Creative BioResearch Group, School of Life Sciences, Kyungpook National University , Daehak-ro 80, Buk-ku, Daegu 702-701, Korea.
[Ti] Título:Structural Insights into Substrate Specificity of Cystathionine γ-Synthase from Corynebacterium glutamicum.
[So] Source:J Agric Food Chem;65(29):6002-6008, 2017 Jul 26.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cystathionine γ-synthase (MetB) condenses O-acetyl-l-homoserine (OAHS) or O-succinyl-l-homoserine (OSHS) with cysteine to produce cystathionine. To investigate the molecular mechanisms and substrate specificity of MetB from Corynebacterium glutamicum (CgMetB), we determined its crystal structure at 1.5 Å resolution. The pyridoxal phosphate cofactor is covalently bound to Lys204 via a Schiff base linkage in the deep cavity. Superposition with the structure of MetB from Nicotiana tabacum in complex with its inhibitor dl-(E)-2-amino-5-phosphono-3-pentenoic acid revealed that Thr347 from the ß10-ß11 connecting loop, located at the entrance of the active site, is speculated to be a main contributor for stabilization of the acetyl group of OAHS. Moreover, on the basis of structural comparison of CgMetB with EcMetB utilizing OSHS as a main substrate, we propose that the conformation of the ß10-ß11 connecting loops determines the size and shape of the acetyl- or succinyl-group binding site and ultimately determines the substrate specificity of MetBs toward OAHS or OSHS.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Carbono-Oxigênio Liases/química
Corynebacterium glutamicum/enzimologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Carbono-Oxigênio Liases/genética
Carbono-Oxigênio Liases/metabolismo
Domínio Catalítico
Corynebacterium glutamicum/química
Corynebacterium glutamicum/genética
Homosserina/análogos & derivados
Homosserina/química
Homosserina/metabolismo
Cinética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 1492-23-5 (O-succinylhomoserine); 6KA95X0IVO (Homoserine); EC 2.5.1.48 (O-succinylhomoserine (thiol)-lyase); EC 4.2.- (Carbon-Oxygen Lyases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170809
[Lr] Data última revisão:
170809
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170705
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b02391


  3 / 815 MEDLINE  
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[PMID]:28325837
[Au] Autor:Meijer BM; Jang SM; Guerrera IC; Chhuon C; Lipecka J; Reisacher C; Baleux F; Sansonetti PJ; Muchardt C; Arbibe L
[Ad] Endereço:From the Team genomic plasticity and infection, Department of Immunology, Infectiology and Hematology, Institut Necker Enfants Malades, INSERM U1151, CNRS UMR 8253, 75993 Paris CEDEX 14, France.
[Ti] Título:Threonine eliminylation by bacterial phosphothreonine lyases rapidly causes cross-linking of mitogen-activated protein kinase (MAPK) in live cells.
[So] Source:J Biol Chem;292(19):7784-7794, 2017 May 12.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Old long-lived proteins contain dehydroalanine (Dha) and dehydrobutyrine (Dhb), two amino acids engendered by dehydration of serines and threonines, respectively. Although these residues have a suspected role in protein cross-linking and aggregation, their direct implication has yet to be determined. Here, we have taken advantage of the ability of the enteropathogen to convert the phosphothreonine residue of the pT- -pY consensus sequence of ERK and p38 into Dhb and followed the impact of dehydration on the fate of the two MAPKs. To that end, we have generated the first antibodies recognizing Dhb-modified proteins and allowing tracing them as they form. We showed that Dhb modifications accumulate in a long-lasting manner -infected cells, causing subsequent formation of covalent cross-links of MAPKs. Moreover, the Dhb signal correlates precisely with the activation of the type III secretion apparatus, thus evidencing injectisome activity. This observation is the first to document a causal link between Dhb formation and protein cross-linking in live cells. Detection of eliminylation is a new avenue to phosphoproteome regulation in eukaryotes that will be instrumental for the development of type III secretion inhibitors.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Carbono-Oxigênio Liases/metabolismo
Sistema de Sinalização das MAP Quinases
Shigella/enzimologia
Treonina/química
[Mh] Termos MeSH secundário: Alanina/análogos & derivados
Alanina/química
Aminobutiratos/química
Animais
Anticorpos/química
Células CACO-2
Linhagem Celular
MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Células HeLa
Seres Humanos
Camundongos
Ligação Proteica
Proteômica
Especificidade por Substrato
Sistemas de Secreção Tipo III
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aminobutyrates); 0 (Antibodies); 0 (Bacterial Proteins); 0 (Type III Secretion Systems); 20748-08-7 (dehydrobutyrine); 2ZD004190S (Threonine); 98RA387EKY (dehydroalanine); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases); EC 4.2.- (Carbon-Oxygen Lyases); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170323
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.775940


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[PMID]:28294619
[Au] Autor:Kumar P; Jander G
[Ad] Endereço:Boyce Thompson Institute for Plant Research , 533 Tower Road, Ithaca, New York 14853, United States.
[Ti] Título:Concurrent Overexpression of Arabidopsis thaliana Cystathionine γ-Synthase and Silencing of Endogenous Methionine γ-Lyase Enhance Tuber Methionine Content in Solanum tuberosum.
[So] Source:J Agric Food Chem;65(13):2737-2742, 2017 Apr 05.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Potatoes (Solanum tuberosum) are deficient in methionine, an essential amino acid in human and animal diets. Higher methionine levels increase the nutritional quality and promote the typically pleasant aroma associated with baked and fried potatoes. Several attempts have been made to elevate tuber methionine levels by genetic engineering of methionine biosynthesis and catabolism. Overexpressing Arabidopsis thaliana cystathionine γ-synthase (AtCGS) in S. tuberosum up-regulates a rate-limiting step of methionine biosynthesis and increases tuber methionine levels. Alternatively, silencing S. tuberosum methionine γ-lyase (StMGL), which causes decreased degradation of methionine into 2-ketobutyrate, also increases methionine levels. Concurrently enhancing biosynthesis and reducing degradation were predicted to provide further increases in tuber methionine content. Here we report that S. tuberosum cv. Désirée plants with AtCGS overexpression and StMGL silenced by RNA interference are morphologically normal and accumulate higher free methionine levels than either single-transgenic line.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/genética
Arabidopsis/enzimologia
Carbono-Oxigênio Liases/genética
Liases de Carbono-Enxofre/genética
Metionina/metabolismo
Proteínas de Plantas/genética
Plantas Geneticamente Modificadas/metabolismo
Solanum tuberosum/genética
[Mh] Termos MeSH secundário: Proteínas de Arabidopsis/metabolismo
Carbono-Oxigênio Liases/metabolismo
Liases de Carbono-Enxofre/metabolismo
Regulação da Expressão Gênica de Plantas
Engenharia Metabólica
Proteínas de Plantas/metabolismo
Tubérculos/enzimologia
Tubérculos/genética
Tubérculos/crescimento & desenvolvimento
Tubérculos/metabolismo
Plantas Geneticamente Modificadas/enzimologia
Plantas Geneticamente Modificadas/genética
Plantas Geneticamente Modificadas/crescimento & desenvolvimento
Solanum tuberosum/enzimologia
Solanum tuberosum/crescimento & desenvolvimento
Solanum tuberosum/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Plant Proteins); AE28F7PNPL (Methionine); EC 2.5.1.48 (O-succinylhomoserine (thiol)-lyase); EC 4.2.- (Carbon-Oxygen Lyases); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.11 (L-methionine gamma-lyase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170605
[Lr] Data última revisão:
170605
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b00272


  5 / 815 MEDLINE  
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[PMID]:28258000
[Au] Autor:Ed-Dra A; Filali FR; Karraouan B; El Allaoui A; Aboulkacem A; Bouchrif B
[Ad] Endereço:Equipe de Microbiologie et Santé, Laboratoire de Chimie-Biologie Appliquées à l'Environnement, Université Moulay Ismail Faculté des Sciences, B.P. 11201, Zitoune Meknès, Morocco.
[Ti] Título:Prevalence, molecular and antimicrobial resistance of Salmonella isolated from sausages in Meknes, Morocco.
[So] Source:Microb Pathog;105:340-345, 2017 Apr.
[Is] ISSN:1096-1208
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Salmonella is among the most important food borne pathogens worldwide contaminating a wide range of animal products including meat products. The aims of this study go through two steps: The first step is to estimate the proportion of sausages products contaminated with Salmonella in Meknes city (Morocco), which were collected from various shopping sites: butchery, street vendors, supermarket and souk (Weekly market combines the population of the small villages around Meknes city). The second one is to identify serovars, to determine the antimicrobials resistance patterns of isolates and to detect the invA and spvC genes. 34 (21.79%) Salmonella were isolated, recovered 4 serogroups and 12 serotypes. The most prevalent serotypes were Salmonella Corvallis (23.53%) and Salmonella Kentucky (17.65%). All Salmonella isolates were tested for their susceptibility to 18 selected antimicrobials agents, of which 100% were resistant to at least one antimicrobial, 85.30% (29/34) were resistant to two or more antimicrobials and 44.12% (15/34) were resistant to at least three antimicrobials. All Salmonella are resistant to ampicillin, 76.47% to streptomycin, 20.59% to sulfonamides, 17.65% to Tetracycline and 11.77% to Ofloxacin. The "ACSSuT" penta-resistance pattern was observed in tow of the Salmonella Typhimurium strains. In addition, this study showed that all Salmonella strains (34) were positive for invasion gene invA and negative for the virulence gene spvC.
[Mh] Termos MeSH primário: Anti-Infecciosos/farmacologia
Produtos da Carne/microbiologia
Salmonella/efeitos dos fármacos
Salmonella/genética
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/genética
Carbono-Oxigênio Liases
Farmacorresistência Bacteriana Múltipla
Microbiologia de Alimentos/métodos
Genes Bacterianos
Testes de Sensibilidade Microbiana
Marrocos
Prevalência
Salmonella/isolamento & purificação
Salmonella typhimurium/efeitos dos fármacos
Salmonella typhimurium/genética
Salmonella typhimurium/isolamento & purificação
Suínos
Virulência/genética
Fatores de Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Bacterial Proteins); 0 (Virulence Factors); 147652-43-5 (invA protein, Bacteria); EC 4.2.- (Carbon-Oxygen Lyases); EC 4.2.- (phosphothreonine lyase, Salmonella enterica)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170505
[Lr] Data última revisão:
170505
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170305
[St] Status:MEDLINE


  6 / 815 MEDLINE  
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[PMID]:28215610
[Au] Autor:Xu J; Ai Y; Wang J; Xu J; Zhang Y; Yang D
[Ad] Endereço:Gene Engineering and Biotechnology Beijing Key Laboratory, College of Life Sciences, Beijing Normal University, Beijing, 100875 China.
[Ti] Título:Converting S-limonene synthase to pinene or phellandrene synthases reveals the plasticity of the active site.
[So] Source:Phytochemistry;137:34-41, 2017 May.
[Is] ISSN:1873-3700
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:S-limonene synthase is a model monoterpene synthase that cyclizes geranyl pyrophosphate (GPP) to form S-limonene. It is a relatively specific enzyme as the majority of its products are composed of limonene. In this study, we converted it to pinene or phellandrene synthases after introducing N345A/L423A/S454A or N345I mutations. Further studies on N345 suggest the polarity of this residue plays a critical role in limonene production by stabilizing the terpinyl cation intermediate. If it is mutated to a non-polar residue, further cyclization or hydride shifts occurs so the carbocation migrates towards the pyrophosphate, leading to the production of pinene or phellandrene. On the other hand, mutant enzymes that still possess a polar residue at this position produce limonene as the major product. N345 is not the only polar residue that may stabilize the terpinyl cation because it is not strictly conserved among limonene synthases across species and there are also several other polar residues in this area. These residues could form a "polar pocket" that may collectively play this stabilizing role. Our study provides important insights into the catalytic mechanism of limonene synthases. Furthermore, it also has wider implications on the evolution of terpene synthases.
[Mh] Termos MeSH primário: Carbono-Oxigênio Liases/química
Liases Intramoleculares/química
[Mh] Termos MeSH secundário: Carbono-Oxigênio Liases/genética
Domínio Catalítico
Cicloexenos/química
Liases Intramoleculares/genética
Mentha spicata/enzimologia
Mentha spicata/genética
Modelos Moleculares
Mutagênese
Mutação
Fosfatos de Poli-Isoprenil/química
Terpenos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyclohexenes); 0 (Polyisoprenyl Phosphates); 0 (Terpenes); 763-10-0 (geranyl pyrophosphate); 9MC3I34447 (limonene); EC 4.2.- (Carbon-Oxygen Lyases); EC 4.2.3.119 ((-)-alpha-pinene synthase); EC 5.5.- (Intramolecular Lyases); EC 5.5.- (pinene cyclase I)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170407
[Lr] Data última revisão:
170407
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170221
[St] Status:MEDLINE


  7 / 815 MEDLINE  
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[PMID]:28194610
[Au] Autor:Lu D; Pang G; Xie J
[Ad] Endereço:Biotechnology & Food Science College, Tianjin University of Commerce, Tianjin, 300314, China.
[Ti] Título:A new phosphothreonine lyase electrochemical immunosensor for detecting Salmonella based on horseradish peroxidase/GNPs-thionine/chitosan.
[So] Source:Biomed Microdevices;19(1):12, 2017 Mar.
[Is] ISSN:1572-8781
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the current study, a novel double-layer gold nanoparticles- electrochemical immunosensor electrode (DGN-EIE) immobilized with Salmonella plasmid virulence C (SpvC) antibody was developed. To increase the fixed quantity of antibodies and electrochemical signal, an electrochemical biosensing signal amplification system was utilized with gold nanoparticles-thionine-chitosan absorbing horseradish peroxidase (HRP). In addition, the SpvC monoclonal antibodies (derived from Balb/c mice) were prepared and screened with a high affinity to SpvC. To evaluate the quality of DGN-EIE, the amperometric I-t curve method was applied to determine Salmonella in PBS. The results showed that the response current had a good linear correlation with the bacterial quantity ranged from 1.0 × 10 -5.0 × 10 cfu/mL. The lowest detection limit was found at 5 cfu/mL. Furthermore, the proposed immunosensor has been demonstrated with high sensitivity, good selectivity and reproducibility. Apparently, DGN-EIE may be a very useful tool for monitoring the bacteria.
[Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos
Carbono-Oxigênio Liases/imunologia
Quitosana/química
Ouro/química
Peroxidase do Rábano Silvestre/metabolismo
Fenotiazinas/química
Salmonella/isolamento & purificação
[Mh] Termos MeSH secundário: Anticorpos Imobilizados/química
Anticorpos Imobilizados/imunologia
Técnicas Biossensoriais/instrumentação
Eletroquímica
Eletrodos
Peroxidase do Rábano Silvestre/química
Imunoensaio
Limite de Detecção
Nanopartículas Metálicas/química
Salmonella/enzimologia
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Immobilized); 0 (Phenothiazines); 7440-57-5 (Gold); 9012-76-4 (Chitosan); EC 1.11.1.- (Horseradish Peroxidase); EC 4.2.- (Carbon-Oxygen Lyases); VTT2SAT5H0 (thionine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170215
[St] Status:MEDLINE
[do] DOI:10.1007/s10544-017-0149-4


  8 / 815 MEDLINE  
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[PMID]:27844098
[Au] Autor:Rose P; Moore PK; Zhu YZ
[Ad] Endereço:School of Life Science, University of Lincoln, Brayford Pool, Lincoln, Lincolnshire, LN6 7TS, UK. prose@lincoln.ac.uk.
[Ti] Título:H S biosynthesis and catabolism: new insights from molecular studies.
[So] Source:Cell Mol Life Sci;74(8):1391-1412, 2017 Apr.
[Is] ISSN:1420-9071
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Hydrogen sulfide (H S) has profound biological effects within living organisms and is now increasingly being considered alongside other gaseous signalling molecules, such as nitric oxide (NO) and carbon monoxide (CO). Conventional use of pharmacological and molecular approaches has spawned a rapidly growing research field that has identified H S as playing a functional role in cell-signalling and post-translational modifications. Recently, a number of laboratories have reported the use of siRNA methodologies and genetic mouse models to mimic the loss of function of genes involved in the biosynthesis and degradation of H S within tissues. Studies utilising these systems are revealing new insights into the biology of H S within the cardiovascular system, inflammatory disease, and in cell signalling. In light of this work, the current review will describe recent advances in H S research made possible by the use of molecular approaches and genetic mouse models with perturbed capacities to generate or detoxify physiological levels of H S gas within tissues.
[Mh] Termos MeSH primário: Vias Biossintéticas
Sulfeto de Hidrogênio/metabolismo
[Mh] Termos MeSH secundário: Animais
Carbono-Oxigênio Liases/genética
Carbono-Oxigênio Liases/metabolismo
Cistationina beta-Sintase/genética
Cistationina beta-Sintase/metabolismo
Cisteína Dioxigenase/genética
Cisteína Dioxigenase/metabolismo
Dioxigenases/genética
Dioxigenases/metabolismo
Regulação da Expressão Gênica
Técnicas de Inativação de Genes/métodos
Seres Humanos
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
Quinona Redutases/genética
Quinona Redutases/metabolismo
Transdução de Sinais
Sulfurtransferases/genética
Sulfurtransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Mitochondrial Proteins); EC 1.13.11.- (Dioxygenases); EC 1.13.11.18 (ETHE1 protein, mouse); EC 1.13.11.20 (Cysteine Dioxygenase); EC 1.6.99.- (Quinone Reductases); EC 1.8.5.- (sulfide quinone reductase); EC 2.5.1.48 (O-succinylhomoserine (thiol)-lyase); EC 2.8.1.- (Sulfurtransferases); EC 2.8.1.2 (3-mercaptopyruvate sulphurtransferase); EC 4.2.- (Carbon-Oxygen Lyases); EC 4.2.1.22 (Cystathionine beta-Synthase); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161116
[St] Status:MEDLINE
[do] DOI:10.1007/s00018-016-2406-8


  9 / 815 MEDLINE  
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[PMID]:27367317
[Au] Autor:Hou M; Chen R; Yang D; Núñez G; Wang Z; Wang Q; Zhang Y; Liu Q
[Ad] Endereço:State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, 200237, China.
[Ti] Título:Identification and functional characterization of EseH, a new effector of the type III secretion system of Edwardsiella piscicida.
[So] Source:Cell Microbiol;19(1), 2017 Jan.
[Is] ISSN:1462-5822
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Edwardsiella piscicida, a bacterial pathogen in fish and humans, expresses a type III secretion system (T3SS) that is critical for pathogen virulence and disease development. However, little is known about the associated effectors and their functional importance. In this study, we identified the ETAE_1757 encoded protein, termed here E. piscicida secretion effector H (EseH) as a novel T3SS effector. We found that upon infection with E. piscicida, EseH is translocated into nucleus of host cells which required the T3SS. Homology modelling analysis suggests that EseH is an enzyme that belongs to the family of phosphothreothine lyases. Consistently, EseH inhibited phosphorylation of ERK1/2, p38α and JNK MAPK pathways in host cells, but had no effect on the NF-kB pathway. Furthermore, mutation of the critical amino acid residues predicted to confer phosphothreonine lyase activity abolished the ability of EseH to inhibit phosphorylation of ERK1/2, p38α and JNK MAPK pathways in host cells. In addition, we found an increase in transcript levels of TNF-α, IL-12, IL-10 and IFN-γ in zebrafish infected with the eseH mutant when compared with the wild type bacterium. Importantly, the virulence of E. piscicida deficient in EseH was highly attenuated in the zebrafish infection model which correlated with decreased loads of the mutant bacterium in both liver and kidney. Complementation of the E. piscicida mutant strain with EseH restored virulence in zebrafish. These results identified EseH as a critical T3SS effector that contributes to virulence by targeting MAPK signalling during E. piscicida infection.
[Mh] Termos MeSH primário: Carbono-Oxigênio Liases/metabolismo
Edwardsiella/genética
Edwardsiella/patogenicidade
Interações Hospedeiro-Patógeno
Sistemas de Secreção Tipo III/metabolismo
Fatores de Virulência/metabolismo
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Substituição de Aminoácidos
Animais
Carga Bacteriana
Carbono-Oxigênio Liases/genética
Núcleo Celular/química
Citocinas/análise
Análise Mutacional de DNA
Modelos Animais de Doenças
Infecções por Enterobacteriaceae/microbiologia
Infecções por Enterobacteriaceae/patologia
Técnicas de Inativação de Genes
Teste de Complementação Genética
Evasão da Resposta Imune
Rim/microbiologia
Fígado/microbiologia
Quinases de Proteína Quinase Ativadas por Mitógeno/antagonistas & inibidores
Homologia de Sequência de Aminoácidos
Transdução de Sinais
Virulência
Fatores de Virulência/genética
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Type III Secretion Systems); 0 (Virulence Factors); EC 2.7.12.2 (Mitogen-Activated Protein Kinase Kinases); EC 4.2.- (Carbon-Oxygen Lyases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170802
[Lr] Data última revisão:
170802
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160702
[St] Status:MEDLINE
[do] DOI:10.1111/cmi.12638


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[PMID]:27608544
[Au] Autor:Atabakhshi-Kashi M; Mohammadi M; Mirhassani R; Dabirmanesh B; Sajedi RH; Khajeh K
[Ad] Endereço:Department of Biochemistry, Faculty of Biological Science, Tarbiat Modares University, Tehran 14115-175, Iran.
[Ti] Título:An alternative allosteric pathway in thermophilic methylglyoxal synthase.
[So] Source:Int J Biol Macromol;93(Pt A):526-533, 2016 Dec.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Methylglyoxal synthase (MGS) is a homohexameric enzyme responsible for converting dihydroxyacetone phosphate (DHAP) to methylglyoxal and phosphate in the methylglyoxal bypass of glycolysis. Phosphate acts as an allosteric inhibitor and strong regulator for this enzyme. Previous studies on MGS from Thermus sp. GH5 (TMGS) had indicated a pathway for transmitting the signal through Pro82, Arg97 and Val101 to the active site. The necessity of these residues for heterotropic negative cooperativity between subunits of TMGS were also proposed. In this study, it has been shown that a path via a salt bridge between Arg80 and Asp100 in the narrow dimer interface provides an alternative pathway for transmission of the allosteric inhibitory signal through subunit interfaces.
[Mh] Termos MeSH primário: Carbono-Oxigênio Liases/química
Carbono-Oxigênio Liases/metabolismo
Temperatura Ambiente
Thermus/enzimologia
[Mh] Termos MeSH secundário: Regulação Alostérica/efeitos dos fármacos
Sequência de Aminoácidos
Carbono-Oxigênio Liases/genética
Estabilidade Enzimática
Ligações de Hidrogênio
Interações Hidrofóbicas e Hidrofílicas
Cinética
Modelos Moleculares
Fosfatos/farmacologia
Estrutura Secundária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phosphates); EC 4.2.- (Carbon-Oxygen Lyases); EC 4.2.3.3 (methylglyoxal synthase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170404
[Lr] Data última revisão:
170404
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160910
[St] Status:MEDLINE



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