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[PMID]:28257519
[Au] Autor:Jõesaar M; Viggor S; Heinaru E; Naanuri E; Mehike M; Leito I; Heinaru A
[Ad] Endereço:Institute of Molecular and Cell Biology, Faculty of Science and Technology, University of Tartu, Tartu, Estonia.
[Ti] Título:Strategy of Pseudomonas pseudoalcaligenes C70 for effective degradation of phenol and salicylate.
[So] Source:PLoS One;12(3):e0173180, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phenol- and naphthalene-degrading indigenous Pseudomonas pseudoalcaligenes strain C70 has great potential for the bioremediation of polluted areas. It harbours two chromosomally located catechol meta pathways, one of which is structurally and phylogenetically very similar to the Pseudomonas sp. CF600 dmp operon and the other to the P. stutzeri AN10 nah lower operon. The key enzymes of the catechol meta pathway, catechol 2,3-dioxygenase (C23O) from strain C70, PheB and NahH, have an amino acid identity of 85%. The metabolic and regulatory phenotypes of the wild-type and the mutant strain C70ΔpheB lacking pheB were evaluated. qRT-PCR data showed that in C70, the expression of pheB- and nahH-encoded C23O was induced by phenol and salicylate, respectively. We demonstrate that strain C70 is more effective in the degradation of phenol and salicylate, especially at higher substrate concentrations, when these compounds are present as a mixture; i.e., when both pathways are expressed. Moreover, NahH is able to substitute for the deleted PheB in phenol degradation when salicylate is also present in the growth medium. The appearance of a yellow intermediate 2-hydroxymuconic semialdehyde was followed by the accumulation of catechol in salicylate-containing growth medium, and lower expression levels and specific activities of the C23O of the sal operon were detected. However, the excretion of the toxic intermediate catechol to the growth medium was avoided when the growth medium was supplemented with phenol, seemingly due to the contribution of the second meta pathway encoded by the phe genes.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Biodegradação Ambiental
Catecol 2,3-Dioxigenase/genética
Fenol/metabolismo
Salicilatos/metabolismo
[Mh] Termos MeSH secundário: Sequência de Bases
Catecol 2,3-Dioxigenase/biossíntese
Catecóis/metabolismo
Regulação Bacteriana da Expressão Gênica
Regulação Enzimológica da Expressão Gênica
Regiões Promotoras Genéticas
Pseudomonas pseudoalcaligenes/enzimologia
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Catechols); 0 (Salicylates); 339NCG44TV (Phenol); EC 1.13.11.2 (Catechol 2,3-Dioxygenase); LF3AJ089DQ (catechol)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170304
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0173180


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[PMID]:28253357
[Au] Autor:Ibáñez MI; Cabello P; Luque-Almagro VM; Sáez LP; Olaya A; Sánchez de Medina V; Luque de Castro MD; Moreno-Vivián C; Roldán MD
[Ad] Endereço:Departamento de Bioquímica y Biología Molecular, Edificio Severo Ochoa, Campus de Rabanales, Universidad de Córdoba, Córdoba, Spain.
[Ti] Título:Quantitative proteomic analysis of Pseudomonas pseudoalcaligenes CECT5344 in response to industrial cyanide-containing wastewaters using Liquid Chromatography-Mass Spectrometry/Mass Spectrometry (LC-MS/MS).
[So] Source:PLoS One;12(3):e0172908, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Biological treatments to degrade cyanide are a powerful technology for cyanide removal from industrial wastewaters. It has been previously demonstrated that the alkaliphilic bacterium Pseudomonas pseudoalcaligenes CECT5344 is able to use free cyanide and several metal-cyanide complexes as the sole nitrogen source. In this work, the strain CECT5344 has been used for detoxification of the different chemical forms of cyanide that are present in alkaline wastewaters from the jewelry industry. This liquid residue also contains large concentrations of metals like iron, copper and zinc, making this wastewater even more toxic. To elucidate the molecular mechanisms involved in the bioremediation process, a quantitative proteomic analysis by LC-MS/MS has been carried out in P. pseudoalcaligenes CECT5344 cells grown with the jewelry residue as sole nitrogen source. Different proteins related to cyanide and cyanate assimilation, as well as other proteins involved in transport and resistance to metals were induced by the cyanide-containing jewelry residue. GntR-like regulatory proteins were also induced by this industrial residue and mutational analysis revealed that GntR-like regulatory proteins may play a role in the regulation of cyanide assimilation in P. pseudoalcaligenes CECT5344. The strain CECT5344 has been used in a batch reactor to remove at pH 9 the different forms of cyanide present in industrial wastewaters from the jewelry industry (0.3 g/L, ca. 12 mM total cyanide, including both free cyanide and metal-cyanide complexes). This is the first report describing the biological removal at alkaline pH of such as elevated concentration of cyanide present in a heterogeneous mixture from an industrial source.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Cromatografia Líquida/métodos
Cianetos/toxicidade
Proteômica
Pseudomonas pseudoalcaligenes/efeitos dos fármacos
Espectrometria de Massas em Tandem/métodos
Águas Residuais/química
[Mh] Termos MeSH secundário: Biodegradação Ambiental
Reatores Biológicos
Genes Bacterianos
Pseudomonas pseudoalcaligenes/genética
Pseudomonas pseudoalcaligenes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cyanides); 0 (Waste Water)
[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:170303
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0172908


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[PMID]:28235872
[Au] Autor:Acera F; Carmona MI; Castillo F; Quesada A; Blasco R
[Ad] Endereço:Departamento de Bioquímica, Biología Molecular y Genética, Facultad de Veterinaria, Universidad de Extremadura, Cáceres, Spain.
[Ti] Título:A Cyanide-Induced 3-Cyanoalanine Nitrilase in the Cyanide-Assimilating Bacterium Pseudomonas pseudoalcaligenes Strain CECT 5344.
[So] Source:Appl Environ Microbiol;83(9), 2017 May 01.
[Is] ISSN:1098-5336
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CECT 5344 is a bacterium able to assimilate cyanide as a sole nitrogen source. Under this growth condition, a 3-cyanoalanine nitrilase enzymatic activity was induced. This activity was encoded by , one of the four nitrilase genes detected in the genome of this bacterium, and its expression in enabled the recombinant strain to fully assimilate 3-cyanoalanine. CECT 5344 showed a weak growth level with 3-cyanoalanine as the N source, unless KCN was also added. Moreover, a knockout mutant of CECT 5344 became severely impaired in its ability to grow with 3-cyanoalanine and cyanide as nitrogen sources. The native enzyme expressed in was purified up to electrophoretic homogeneity and biochemically characterized. Nit4 seems to be specific for 3-cyanoalanine, and the amount of ammonium derived from the enzymatic activity doubled in the presence of exogenously added asparaginase activity, which demonstrated that the Nit4 enzyme had both 3-cyanoalanine nitrilase and hydratase activities. The gene is located downstream of the cyanide resistance transcriptional unit containing genes, whose expression levels are under the positive control of cyanide. Real-time PCR experiments revealed that expression was also positively regulated by cyanide in both minimal and LB media. These results suggest that this gene cluster including and could be involved both in cyanide resistance and in its assimilation by CECT 5344. Cyanide is a highly toxic molecule present in some industrial wastes due to its application in several manufacturing processes, such as gold mining and the electroplating industry. The biodegradation of cyanide from contaminated wastes could be an attractive alternative to physicochemical treatment. CECT 5344 is a bacterial strain able to assimilate cyanide under alkaline conditions, thus avoiding its volatilization as HCN. This paper describes and characterizes an enzyme (Nit4) induced by cyanide that is probably involved in cyanide assimilation. The biochemical characterization of Nit4 provides a segment for building a cyanide assimilation pathway in This information could be useful for understanding, and hopefully improving, the mechanisms involved in bacterial cyanide biodegradation and its application in the treatment of cyanide-containing wastes.
[Mh] Termos MeSH primário: Alanina/análogos & derivados
Aminoidrolases/metabolismo
Cianetos/metabolismo
Hidroliases/metabolismo
Pseudomonas pseudoalcaligenes/enzimologia
Pseudomonas pseudoalcaligenes/metabolismo
Ativação Transcricional
[Mh] Termos MeSH secundário: Alanina/metabolismo
Aminoidrolases/genética
Aminoidrolases/isolamento & purificação
Compostos de Amônio/metabolismo
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Técnicas de Inativação de Genes
Hidroliases/genética
Hidroliases/isolamento & purificação
Nitrogênio/metabolismo
Pseudomonas pseudoalcaligenes/genética
Pseudomonas pseudoalcaligenes/crescimento & desenvolvimento
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ammonium Compounds); 0 (Cyanides); 0 (Recombinant Proteins); 923-01-3 (3-cyanoalanine); EC 3.5.4.- (Aminohydrolases); EC 3.5.5.1 (nitrilase); EC 4.2.1.- (Hydro-Lyases); EC 4.2.1.65 (3-cyanoalanine hydratase); N762921K75 (Nitrogen); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170226
[St] Status:MEDLINE


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[PMID]:27872998
[Au] Autor:Wallace PW; Haernvall K; Ribitsch D; Zitzenbacher S; Schittmayer M; Steinkellner G; Gruber K; Guebitz GM; Birner-Gruenberger R
[Ad] Endereço:Research Unit for Functional Proteomics and Metabolic Pathways, Institute of Pathology, Medical University of Graz, Stiftingtalstrasse 24, 8010, Graz, Austria.
[Ti] Título:PpEst is a novel PBAT degrading polyesterase identified by proteomic screening of Pseudomonas pseudoalcaligenes.
[So] Source:Appl Microbiol Biotechnol;101(6):2291-2303, 2017 Mar.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A novel esterase, PpEst, that hydrolyses the co-aromatic-aliphatic polyester poly(1,4-butylene adipate-co-terephthalate) (PBAT) was identified by proteomic screening of the Pseudomonas pseudoalcaligenes secretome. PpEst was induced by the presence of PBAT in the growth media and had predicted arylesterase (EC 3.1.1.2) activity. PpEst showed polyesterase activity on both whole and milled PBAT film releasing terephthalic acid and 4-(4-hydroxybutoxycarbonyl)benzoic acid while end product inhibition by 4-(4-hydroxybutoxycarbonyl)benzoic acid was observed. Modelling of an aromatic polyester mimicking oligomer into the PpEst active site indicated that the binding pocket could be big enough to accommodate large polymers. This is the first report of a PBAT degrading enzyme being identified by proteomic screening and shows that this approach can contribute to the discovery of new polymer hydrolysing enzymes. Moreover, these results indicate that arylesterases could be an interesting enzyme class for identifications of polyesterases.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Plásticos Biodegradáveis/metabolismo
Hidrolases de Éster Carboxílico/química
Poliésteres/metabolismo
Pseudomonas pseudoalcaligenes/enzimologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Plásticos Biodegradáveis/química
Hidrolases de Éster Carboxílico/genética
Hidrolases de Éster Carboxílico/metabolismo
Domínio Catalítico
Expressão Gênica
Modelos Moleculares
Ácidos Ftálicos/química
Ácidos Ftálicos/metabolismo
Poliésteres/química
Ligação Proteica
Proteômica
Pseudomonas pseudoalcaligenes/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Biodegradable Plastics); 0 (Phthalic Acids); 0 (Polyesters); 0 (poly(butylene adipate-co-butylene terephthalate)); 6S7NKZ40BQ (terephthalic acid); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.2 (arylesterase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170307
[Lr] Data última revisão:
170307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161123
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-016-7992-8


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[PMID]:27151656
[Au] Autor:Fedi S; Barberi TT; Nappi MR; Sandri F; Booth S; Turner RJ; Attimonelli M; Cappelletti M; Zannoni D
[Ad] Endereço:Department of Pharmacy and Biotechnology, University of Bologna.
[Ti] Título:The Role of cheA Genes in Swarming and Swimming Motility of Pseudomonas pseudoalcaligenes KF707.
[So] Source:Microbes Environ;31(2):169-72, 2016 Jun 25.
[Is] ISSN:1347-4405
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:A genome analysis of Pseudomonas pseudoalcaligenes KF707, a PCBs degrader and metal-resistant soil microorganism, revealed the presence of two novel gene clusters named che2 and che3, which were predicted to be involved in chemotaxis-like pathways, in addition to a che1 gene cluster. We herein report that the histidine kinase coding genes, cheA2 and cheA3, have no role in swimming or chemotaxis in P. pseudoalcaligenes KF707, in contrast to cheA1. However, the cheA1 and cheA2 genes were both necessary for cell swarming, whereas the cheA3 gene product had a negative effect on the optimal swarming phenotype of KF707 cells.
[Mh] Termos MeSH primário: Histidina Quinase/metabolismo
Proteínas Quimiotáticas Aceptoras de Metil/metabolismo
Pseudomonas pseudoalcaligenes/genética
Pseudomonas pseudoalcaligenes/fisiologia
[Mh] Termos MeSH secundário: Histidina Quinase/genética
Locomoção
Proteínas Quimiotáticas Aceptoras de Metil/genética
Família Multigênica
Pseudomonas pseudoalcaligenes/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Methyl-Accepting Chemotaxis Proteins); EC 2.7.13.1 (Histidine Kinase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160507
[St] Status:MEDLINE
[do] DOI:10.1264/jsme2.ME15164


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[PMID]:27060556
[Au] Autor:Wibberg D; Bremges A; Dammann-Kalinowski T; Maus I; Igeño MI; Vogelsang R; König C; Luque-Almagro VM; Roldán MD; Sczyrba A; Moreno-Vivián C; Blasco R; Pühler A; Schlüter A
[Ad] Endereço:Institute for Genome Research and Systems Biology, Center for Biotechnology (CeBiTec), Bielefeld University, D-33615 Bielefeld, Germany.
[Ti] Título:Finished genome sequence and methylome of the cyanide-degrading Pseudomonas pseudoalcaligenes strain CECT5344 as resolved by single-molecule real-time sequencing.
[So] Source:J Biotechnol;232:61-8, 2016 Aug 20.
[Is] ISSN:1873-4863
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Pseudomonas pseudoalcaligenes CECT5344 tolerates cyanide and is also able to utilize cyanide and cyano-derivatives as a nitrogen source under alkaline conditions. The strain is considered as candidate for bioremediation of habitats contaminated with cyanide-containing liquid wastes. Information on the genome sequence of the strain CECT5344 became available previously. The P. pseudoalcaligenes CECT5344 genome was now resequenced by applying the single molecule, real-time (SMRT(®)) sequencing technique developed by Pacific Biosciences. The complete and finished genome sequence of the strain consists of a 4,696,984 bp chromosome featuring a GC-content of 62.34%. Comparative analyses between the new and previous versions of the P. pseudoalcaligenes CECT5344 genome sequence revealed additional regions in the new sequence that were missed in the older version. These additional regions mostly represent mobile genetic elements. Moreover, five additional genes predicted to play a role in sulfoxide reduction are present in the newly established genome sequence. The P. pseudoalcaligenes CECT5344 genome sequence is highly related to the genome sequences of different Pseudomonas mendocina strains. Approximately, 70% of all genes are shared between P. pseudoalcaligenes and P. mendocina. In contrast to P. mendocina, putative pathogenicity genes were not identified in the P. pseudoalcaligenes CECT5344 genome. P. pseudoalcaligenes CECT5344 possesses unique genes for nitrilases and mercury resistance proteins that are of importance for survival in habitats contaminated with cyano- and mercury compounds. As an additional feature of the SMRT sequencing technology, the methylome of P. pseudoalcaligenes was established. Six sequence motifs featuring methylated adenine residues (m6A) were identified in the genome. The genome encodes several methyltransferases, some of which may be considered for methylation of the m6A motifs identified. The complete genome sequence of the strain CECT5344 now provides the basis for exploitation of genetic features for biotechnological purposes.
[Mh] Termos MeSH primário: Cianetos/metabolismo
Genoma Bacteriano/genética
Pseudomonas pseudoalcaligenes/genética
Pseudomonas pseudoalcaligenes/metabolismo
Análise de Sequência de DNA/métodos
[Mh] Termos MeSH secundário: Metilação de DNA
DNA Bacteriano/análise
DNA Bacteriano/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyanides); 0 (DNA, Bacterial)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170227
[Lr] Data última revisão:
170227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160410
[St] Status:MEDLINE


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[PMID]:26857610
[Au] Autor:Wei Y; Xia S; He C; Xiong W; Xu H
[Ad] Endereço:College of Bioinformatics, Chongqing University of Posts and Telecommunications, Chongqing, 400065, People's Republic of China.
[Ti] Título:Highly enantioselective production of a chiral intermediate of sitagliptin by a novel isolate of Pseudomonas pseudoalcaligenes.
[So] Source:Biotechnol Lett;38(5):841-6, 2016 May.
[Is] ISSN:1573-6776
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To produce (S)-3-hydroxy-1-(3-(trifluoromethyl)-5,6-dihydro[1,2,4]triazolo[4,3-a]pyrazin-7(8H)-yl]-4-(2,4,5-trifluorophenyl)butan-1-one (S)-1 from 4-oxo-4-[3-(trifluoromethyl)-5,6-dihydro [1,2,4]triazolo[4,3-a]pyrazin-7(8H)-yl)-1-(2,4,5-trifluorophenyl)butan-2-one (2) by microbial bioreduction. RESULTS: A new isolate of Pseudomonas pseudoalcaligenes reduced enantioselectively prochiral ketone 2 to chiral alcohol (S)-1. Whole cells of the bacterium were tolerant towards 20 % (v/v) DMSO and 10 g 2/l. Under the optimal conditions, the preparative-scale bioreduction yielded (S)-1 at 90 % yield and >99 % ee. Cells could be re-used with the yield and ee of product being 45 % and >99 %, respectively, after five cycles. CONCLUSION: Bioreduction using whole cells of P. pseudoalcaligenes is an attractive approach to produce (S)-1, as a chiral intermediate of the anti-diabetic drug, sitagliptin.
[Mh] Termos MeSH primário: Pseudomonas pseudoalcaligenes/metabolismo
Fosfato de Sitagliptina/metabolismo
Estereoisomerismo
[Mh] Termos MeSH secundário: Oxirredução
Fosfato de Sitagliptina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
TS63EW8X6F (Sitagliptin Phosphate)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160210
[St] Status:MEDLINE
[do] DOI:10.1007/s10529-016-2051-1


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[PMID]:26702041
[Au] Autor:Bono LM; Gensel CL; Pfennig DW; Burch CL
[Ad] Endereço:Department of Biology, University of North Carolina, Chapel Hill, NC 27599-3280, USA Department of Ecology and Evolutionary Biology, Yale University, New Haven, CT 06520-8106, USA.
[Ti] Título:Evolutionary rescue and the coexistence of generalist and specialist competitors: an experimental test.
[So] Source:Proc Biol Sci;282(1821):20151932, 2015 12 22.
[Is] ISSN:1471-2954
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Competition for resources is thought to play a critical role in both the origins and maintenance of biodiversity. Although numerous laboratory evolution experiments have confirmed that competition can be a key driver of adaptive diversification, few have demonstrated its role in the maintenance of the resulting diversity. We investigate the conditions that favour the origin and maintenance of alternative generalist and specialist resource-use phenotypes within the same population. Previously, we confirmed that competition for hosts among φ6 bacteriophage in a mixed novel (non-permissive) and ancestral (permissive) host microcosm triggered the evolution of a generalist phenotype capable of infecting both hosts. However, because the newly evolved generalists tended to competitively exclude the ancestral specialists, coexistence between the two phenotypes was rare. Here, we show that reducing the relative abundance of the novel host slowed the increase in frequency of the generalist phenotype, allowing sufficient time for the specialist to further adapt to the ancestral host. This adaptation resulted in 'evolutionary rescue' of the specialists, preventing their competitive exclusion by the generalists. Thus, our results suggest that competition promotes both the origin and maintenance of biodiversity when it is strong enough to favour a novel resource-use phenotype, but weak enough to allow adaptation of both the novel and ancestral phenotypes to their respective niches.
[Mh] Termos MeSH primário: Bacteriófago phi 6/fisiologia
Evolução Biológica
[Mh] Termos MeSH secundário: Adaptação Fisiológica
Bacteriófago phi 6/genética
Bacteriófago phi 6/crescimento & desenvolvimento
Ecossistema
Fenótipo
Pseudomonas pseudoalcaligenes/virologia
Pseudomonas syringae/virologia
Seleção Genética
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170505
[Lr] Data última revisão:
170505
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151225
[St] Status:MEDLINE


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[PMID]:26432339
[Au] Autor:Luque-Almagro VM; Escribano MP; Manso I; Sáez LP; Cabello P; Moreno-Vivián C; Roldán MD
[Ad] Endereço:Departamento de Bioquímica y Biología Molecular, Edificio Severo Ochoa, 1ª Planta, Campus de Rabanales, Universidad de Córdoba, 14071 Córdoba, Spain.
[Ti] Título:DNA microarray analysis of the cyanotroph Pseudomonas pseudoalcaligenes CECT5344 in response to nitrogen starvation, cyanide and a jewelry wastewater.
[So] Source:J Biotechnol;214:171-81, 2015 Nov 20.
[Is] ISSN:1873-4863
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Pseudomonas pseudoalcaligenes CECT5344 is an alkaliphilic bacterium that can use cyanide as nitrogen source for growth, becoming a suitable candidate to be applied in biological treatment of cyanide-containing wastewaters. The assessment of the whole genome sequence of the strain CECT5344 has allowed the generation of DNA microarrays to analyze the response to different nitrogen sources. The mRNA of P. pseudoalcaligenes CECT5344 cells grown under nitrogen limiting conditions showed considerable changes when compared against the transcripts from cells grown with ammonium; up-regulated genes were, among others, the glnK gene encoding the nitrogen regulatory protein PII, the two-component ntrBC system involved in global nitrogen regulation, and the ammonium transporter-encoding amtB gene. The protein coding transcripts of P. pseudoalcaligenes CECT5344 cells grown with sodium cyanide or an industrial jewelry wastewater that contains high concentration of cyanide and metals like iron, copper and zinc, were also compared against the transcripts of cells grown with ammonium as nitrogen source. This analysis revealed the induction by cyanide and the cyanide-rich wastewater of four nitrilase-encoding genes, including the nitC gene that is essential for cyanide assimilation, the cyanase cynS gene involved in cyanate assimilation, the cioAB genes required for the cyanide-insensitive respiration, and the ahpC gene coding for an alkyl-hydroperoxide reductase that could be related with iron homeostasis and oxidative stress. The nitC and cynS genes were also induced in cells grown under nitrogen starvation conditions. In cells grown with the jewelry wastewater, a malate quinone:oxidoreductase mqoB gene and several genes coding for metal extrusion systems were specifically induced.
[Mh] Termos MeSH primário: Cianetos/toxicidade
DNA Bacteriano/análise
Joias
Nitrogênio/metabolismo
Pseudomonas pseudoalcaligenes
Águas Residuais/toxicidade
[Mh] Termos MeSH secundário: DNA Bacteriano/genética
Resíduos Industriais
Análise de Sequência com Séries de Oligonucleotídeos
Pseudomonas pseudoalcaligenes/efeitos dos fármacos
Pseudomonas pseudoalcaligenes/genética
Pseudomonas pseudoalcaligenes/fisiologia
Poluentes Químicos da Água/química
Poluentes Químicos da Água/toxicidade
Purificação da Água
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cyanides); 0 (DNA, Bacterial); 0 (Industrial Waste); 0 (Waste Water); 0 (Water Pollutants, Chemical); N762921K75 (Nitrogen)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:151114
[Lr] Data última revisão:
151114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151004
[St] Status:MEDLINE


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[PMID]:26136595
[Au] Autor:Moniodis A; Hamilton T; Racila E; Cockrill B; McCunney R
[Ad] Endereço:Brigham and Women's Hospital, Division of Pulmonary and Critical Care Medicine, PBB-CA-3, 75 Francis Street, Boston, MA 02115, USA. amoniodis@partners.org.
[Ti] Título:Hypersensitivity pneumonitis in a high school teacher.
[So] Source:Occup Med (Lond);65(7):598-600, 2015 Oct.
[Is] ISSN:1471-8405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Hypersensitivity pneumonitis (HP) is an inflammatory lung disease mediated by an immunological response to an inhaled antigen. Outbreaks of HP have been reported in industrial settings where manufacturing workers are exposed to water-based metalworking fluids (MWFs). Water-based MWFs promote growth of microorganisms and can be easily aerosolized and are thus potential aetiological agents of HP. We present a case of HP caused by exposure to water-based MWF in a vocational high school teacher. Culture of MWF used at his school grew Pseudomonas pseudoalcaligenes. This is the first known report of MWF-induced HP outside an industrial setting. The growth of Pseudomonas spp in this case recalls the earliest reports of the microbiology of MWF-induced HP and suggests that routine bacterial culture may be useful in the diagnosis of HP in workplaces without standard cleaning and biocide regulations.
[Mh] Termos MeSH primário: Alveolite Alérgica Extrínseca/etiologia
Metalurgia
Doenças Profissionais/etiologia
Exposição Ocupacional/efeitos adversos
Pseudomonas pseudoalcaligenes
Professores Escolares
[Mh] Termos MeSH secundário: Alveolite Alérgica Extrínseca/microbiologia
Desinfecção
Seres Humanos
Masculino
Meia-Idade
Doenças Profissionais/microbiologia
Água
Local de Trabalho
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
059QF0KO0R (Water)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150703
[St] Status:MEDLINE
[do] DOI:10.1093/occmed/kqv092



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