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Pesquisa : D08.811.277.040.025.325.249 [Categoria DeCS]
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[PMID]:28284722
[Au] Autor:Carranza G; Angius F; Ilioaia O; Solgadi A; Miroux B; Arechaga I
[Ad] Endereço:Departamento de Biología Molecular and Instituto de Biomedicina y Biotecnología de Cantabria (IBBTEC), Universidad de Cantabria - CSIC - SODERCAN, Santander, Spain.
[Ti] Título:Cardiolipin plays an essential role in the formation of intracellular membranes in Escherichia coli.
[So] Source:Biochim Biophys Acta;1859(6):1124-1132, 2017 06.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mitochondria, chloroplasts and photosynthetic bacteria are characterized by the presence of complex and intricate membrane systems. In contrast, non-photosynthetic bacteria lack membrane structures within their cytoplasm. However, large scale over-production of some membrane proteins, such as the fumarate reductase, the mannitol permease MtlA, the glycerol acyl transferase PlsB, the chemotaxis receptor Tsr or the ATP synthase subunit b, can induce the proliferation of intra cellular membranes (ICMs) in the cytoplasm of Escherichia coli. These ICMs are particularly rich in cardiolipin (CL). Here, we have studied the effect of CL in the generation of these membranous structures. We have deleted the three genes (clsA, clsB and clsC) responsible of CL biosynthesis in E. coli and analysed the effect of these mutations by fluorescent and electron microscopy and by lipid mass spectrometry. We have found that CL is essential in the formation of non-lamellar structures in the cytoplasm of E. coli cells. These results could help to understand the structuration of membranes in E. coli and other membrane organelles, such as mitochondria and ER.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Cardiolipinas/metabolismo
Retículo Endoplasmático/metabolismo
Escherichia coli/metabolismo
Proteínas de Membrana/deficiência
Mitocôndrias/metabolismo
Transferases (Outros Grupos de Fosfato Substituídos)/deficiência
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
ATPases Bacterianas Próton-Translocadoras/genética
ATPases Bacterianas Próton-Translocadoras/metabolismo
Retículo Endoplasmático/ultraestrutura
Escherichia coli/ultraestrutura
Corantes Fluorescentes/química
Deleção de Genes
Expressão Gênica
Isoenzimas/deficiência
Isoenzimas/genética
Proteínas de Membrana/genética
Mitocôndrias/ultraestrutura
Imagem com Lapso de Tempo
Transferases (Outros Grupos de Fosfato Substituídos)/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cardiolipins); 0 (Fluorescent Dyes); 0 (Isoenzymes); 0 (Membrane Proteins); EC 2.7.8.- (Transferases (Other Substituted Phosphate Groups)); EC 2.7.8.- (cardiolipin synthetase); EC 3.6.1.- (Bacterial Proton-Translocating ATPases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170629
[Lr] Data última revisão:
170629
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170313
[St] Status:MEDLINE


  2 / 210 MEDLINE  
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[PMID]:27890618
[Au] Autor:Panfoli I; Ponassi M; Ravera S; Calzia D; Beitia M; Morelli A; Rosano C
[Ad] Endereço:Biochemistry Laboratory, Dept. of Pharmacy, University of Genova, Viale Benedetto XV, 3, 16132 Genova, Italy.
[Ti] Título:Tracking protons from respiratory chain complexes to ATP synthase c-subunit: The critical role of serine and threonine residues.
[So] Source:Biochem Biophys Res Commun;482(4):922-927, 2017 Jan 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:F F -ATP synthase is a multisubunit enzyme responsible for the synthesis of ATP. Among its multiple subunits (8 in E. coli, 17 in yeast S. cerevisiae, 16 in vertebrates), two subunits a and c are known to play a central role controlling the H flow through the inner mitochondrial membrane which allows the subsequent synthesis of ATP, but the pathway followed by H within the two proteins is still a matter of debate. In fact, even though the structure of ATP synthase is now well defined, the molecular mechanisms determining the function of both F and F domains are still largely unknown. In this study, we propose a pathway for proton migration along the ATP synthase by hydrogen-bonded chain mechanism, with a key role of serine and threonine residues, by X-ray diffraction data on the subunit a of E. coli Fo.
[Mh] Termos MeSH primário: ATPases Bacterianas Próton-Translocadoras/química
ATPases Bacterianas Próton-Translocadoras/metabolismo
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/metabolismo
Escherichia coli/metabolismo
Prótons
Serina/metabolismo
Treonina/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Sequência de Aminoácidos
Escherichia coli/química
Seres Humanos
Ligações de Hidrogênio
Modelos Moleculares
Alinhamento de Sequência
Serina/química
Treonina/química
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Protons); 2ZD004190S (Threonine); 452VLY9402 (Serine); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (ATP synthase subunit c, E coli); EC 3.6.1.- (Bacterial Proton-Translocating ATPases); EC 3.6.3.14 (atpB protein, E coli)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161129
[St] Status:MEDLINE


  3 / 210 MEDLINE  
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[PMID]:28001127
[Au] Autor:Sobti M; Smits C; Wong AS; Ishmukhametov R; Stock D; Sandin S; Stewart AG
[Ad] Endereço:Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, Australia.
[Ti] Título:Cryo-EM structures of the autoinhibited ATP synthase in three rotational states.
[So] Source:Elife;5, 2016 Dec 21.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A molecular model that provides a framework for interpreting the wealth of functional information obtained on the F-ATP synthase has been generated using cryo-electron microscopy. Three different states that relate to rotation of the enzyme were observed, with the central stalk's ε subunit in an extended autoinhibitory conformation in all three states. The F motor comprises of seven transmembrane helices and a decameric c-ring and invaginations on either side of the membrane indicate the entry and exit channels for protons. The proton translocating subunit contains near parallel helices inclined by ~30° to the membrane, a feature now synonymous with rotary ATPases. For the first time in this rotary ATPase subtype, the peripheral stalk is resolved over its entire length of the complex, revealing the F attachment points and a coiled-coil that bifurcates toward the membrane with its helices separating to embrace subunit from two sides.
[Mh] Termos MeSH primário: ATPases Bacterianas Próton-Translocadoras/ultraestrutura
Microscopia Crioeletrônica
Escherichia coli/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.1.- (Bacterial Proton-Translocating ATPases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161222
[St] Status:MEDLINE


  4 / 210 MEDLINE  
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[PMID]:27706660
[Au] Autor:Chen W; Liang J; He Z; Jiang W
[Ad] Endereço:Department of Stomatology, Eye & ENT Hospital of FuDan University, Shanghai, China.
[Ti] Título:Preliminary study on total protein extraction methods from Enterococcus faecalis biofilm.
[So] Source:Genet Mol Res;15(3), 2016 Aug 30.
[Is] ISSN:1676-5680
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:Enterococcus faecalis is the major pathogen of post-endodontic disease and refractory periapical periodontitis, and recent research on this species has focused on its pathogenicity. E. faecalis most often causes disease in the form of a biofilm, and total protein expression shows a strong association with its virulence. Therefore, the purpose of our study was to explore different methods of extracting the total proteins of the E. faecalis (ATCC 33186 standard strain) biofilm. The total proteins in the biofilm were extracted using an ultrasonication method with varied parameters, including duration, amplitude setting, period, and duty cycle. After the optimal conditions of ultrasonication were determined based on the protein profile from sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis, the total protein content in the biofilm was detected using the bicinchoninic acid assay, Bradford Coomassie brilliant blue assay, and Lowry assay, and the results were compared and analyzed. The parameters for the optimal conditions of ultrasonication were as follows: a processing duration of 2 min, amplitude setting of 20%, and ultrasonication period of 4 s at a 50% duty cycle. The total protein content was 2299.1 mg/dish when measured by the bicinchoninic assay, 3793.8 mg/dish when measured by the Bradford Coomassie brilliant blue assay, and 1858.0 mg/dish when measured by the Lowry assay. These results demonstrate that the Bradford Coomassie brilliant blue assay is a simple and feasible method for use in detecting the total protein content in a bacterial biofilm.
[Mh] Termos MeSH primário: ATPases Bacterianas Próton-Translocadoras/isolamento & purificação
Biofilmes
Enterococcus faecalis/fisiologia
[Mh] Termos MeSH secundário: ATPases Bacterianas Próton-Translocadoras/metabolismo
Eletroforese em Gel de Poliacrilamida
Sonicação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.1.- (Bacterial Proton-Translocating ATPases)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170303
[Lr] Data última revisão:
170303
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161006
[St] Status:MEDLINE
[do] DOI:10.4238/gmr.15038988


  5 / 210 MEDLINE  
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[PMID]:27177595
[Au] Autor:Papachristos K; Muench SP; Paci E
[Ad] Endereço:Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, England.
[Ti] Título:Characterization of the flexibility of the peripheral stalk of prokaryotic rotary A-ATPases by atomistic simulations.
[So] Source:Proteins;84(9):1203-12, 2016 Sep.
[Is] ISSN:1097-0134
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Rotary ATPases are involved in numerous physiological processes, with the three distinct types (F/A/V-ATPases) sharing functional properties and structural features. The basic mechanism involves the counter rotation of two motors, a soluble ATP hydrolyzing/synthesizing domain and a membrane-embedded ion pump connected through a central rotor axle and a stator complex. Within the A/V-ATPase family conformational flexibility of the EG stators has been shown to accommodate catalytic cycling and is considered to be important to function. For the A-ATPase three EG structures have been reported, thought to represent conformational states of the stator during different stages of rotary catalysis. Here we use long, detailed atomistic simulations to show that those structures are conformers explored through thermal fluctuations, but do not represent highly populated states of the EG stator in solution. We show that the coiled coil tail domain has a high persistence length (∼100 nm), but retains the ability to adapt to different conformational states through the presence of two hinge regions. Moreover, the stator network of the related V-ATPase has been suggested to adapt to subunit interactions in the collar region in addition to the nucleotide occupancy of the catalytic domain. The MD simulations reported here, reinforce this observation showing that the EG stators have enough flexibility to adapt to significantly different structural re-arrangements and accommodate structural changes in the catalytic domain whilst resisting the large torque generated by catalytic cycling. These results are important to understand the role the stators play in the rotary-ATPase mechanism. Proteins 2016; 84:1203-1212. © 2016 The Authors. Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: ATPases Bacterianas Próton-Translocadoras/química
ATPases Mitocondriais Próton-Translocadoras/química
Subunidades Proteicas/química
Thermus thermophilus/química
ATPases Vacuolares Próton-Translocadoras/química
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/química
Biocatálise
Domínio Catalítico
Simulação de Dinâmica Molecular
Análise de Componente Principal
Estrutura Secundária de Proteína
Rotação
Thermus thermophilus/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Subunits); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Bacterial Proton-Translocating ATPases); EC 3.6.1.- (Vacuolar Proton-Translocating ATPases); EC 3.6.3.- (Mitochondrial Proton-Translocating ATPases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160515
[St] Status:MEDLINE
[do] DOI:10.1002/prot.25066


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[PMID]:26513379
[Au] Autor:Mienda BS; Shamsir MS; Md Illias R
[Ad] Endereço:a Bioinformatics Research Group (BIRG), Faculty of Biosciences and Medical Engineering, Department of Biosciences and Health Sciences , Universiti Teknologi Malaysia , 81310 Skudai , Johor Bahru , Malaysia.
[Ti] Título:Model-aided atpE gene knockout strategy in Escherichia coli for enhanced succinic acid production from glycerol.
[So] Source:J Biomol Struct Dyn;34(8):1705-16, 2016 Aug.
[Is] ISSN:1538-0254
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Succinic acid is an important platform chemical with a variety of applications. Model-guided metabolic engineering strategies in Escherichia coli for strain improvement to increase succinic acid production using glucose and glycerol remain largely unexplored. Herein, we report what are, to our knowledge, the first metabolic knockout of the atpE gene to have increased succinic acid production using both glucose and alternative glycerol carbon sources in E. coli. Guided by a genome-scale metabolic model, we engineered the E. coli host to enhance anaerobic production of succinic acid by deleting the atpE gene, thereby generating additional reducing equivalents by blocking H(+) conduction across the mutant cell membrane. This strategy produced 1.58 and .49 g l(-1) of succinic acid from glycerol and glucose substrate, respectively. This work further elucidates a model-guided and/or system-based metabolic engineering, involving only a single-gene deletion strategy for enhanced succinic acid production in E. coli.
[Mh] Termos MeSH primário: ATPases Bacterianas Próton-Translocadoras/genética
ATPases Bacterianas Próton-Translocadoras/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Técnicas de Inativação de Genes
Modelos Biológicos
Ácido Succínico/metabolismo
[Mh] Termos MeSH secundário: Fermentação
Glucose/metabolismo
Glicerol/metabolismo
Redes e Vias Metabólicas
Mutação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (atpE protein, E coli); AB6MNQ6J6L (Succinic Acid); EC 3.6.1.- (Bacterial Proton-Translocating ATPases); IY9XDZ35W2 (Glucose); PDC6A3C0OX (Glycerol)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151030
[St] Status:MEDLINE
[do] DOI:10.1080/07391102.2015.1090341


  7 / 210 MEDLINE  
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[PMID]:26169235
[Au] Autor:Hervé C; Bergot E; Veziris N; Blanc FX
[Ad] Endereço:Service de pneumologie, l'institut du thorax, hôpital G. et R. Laënnec, CHU de Nantes, boulevard Jacques-Monod, 44093 Nantes cedex 1, France.
[Ti] Título:[Tuberculosis in 2015: From diagnosis to the detection of multiresistant cases].
[Ti] Título:La tuberculose en 2015 : du diagnostic à la détection des formes résistantes..
[So] Source:Rev Mal Respir;32(8):784-90, 2015 Oct.
[Is] ISSN:1776-2588
[Cp] País de publicação:France
[La] Idioma:fre
[Ab] Resumo:Incidence of pulmonary tuberculosis, a contagious infectious disease, decreases in France with 4934 reported cases in 2013. Tuberculosis remains a global health problem as smear is positive in only 50% cases and culture methods require time. In such a context, genotypic diagnostic tools such as Xpert® MTB/RIF gained interest. This rapid and simple-to-use nucleic acid amplification test allows a diagnosis in two hours and prevents further invasive investigations in pulmonary and mediastinal tuberculosis. Because of its low sensitivity, it cannot be used in pleural fluid. Indirect immunologic tests are of no use to diagnose active tuberculosis disease. Another current area of interest is the emergence of resistant tuberculosis. In France, approximately 100 cases of multidrug resistant tuberculosis and a few extensively drug resistant tuberculosis have been reported in 2014. Even though these forms of tuberculosis are imported, it is crucial to identify hazardous situations and to optimize care of these patients. Xpert® MTB/RIF is again of marked interest here as it detects rifampin resistance with a 95% sensitivity and a 98% specificity. Interpretation of genotypic tests such as Genotype® MTBDR or Xpert® MTB/RIF depends on known detected mutations, although they do not always have a clinical or phenotypic expression. In multidrug resistant tuberculosis, the new drug bedaquiline obtained approval for temporarily use in combination with other molecules when there is no other treatment option. Results of bedaquiline are encouraging but adverse events like QT prolongation or the development of new specific drug resistance should convince clinicians to use it with caution.
[Mh] Termos MeSH primário: Tuberculose/diagnóstico
[Mh] Termos MeSH secundário: Antituberculosos/farmacologia
Antituberculosos/uso terapêutico
Proteínas de Bactérias/antagonistas & inibidores
ATPases Bacterianas Próton-Translocadoras/antagonistas & inibidores
DNA Bacteriano/genética
DNA Bacteriano/isolamento & purificação
Diarilquinolinas/efeitos adversos
Diarilquinolinas/uso terapêutico
França/epidemiologia
Técnicas de Genotipagem
Seres Humanos
Incidência
Testes de Liberação de Interferon-gama
Testes de Sensibilidade Microbiana
Mycobacterium tuberculosis/genética
Mycobacterium tuberculosis/isolamento & purificação
Técnicas de Amplificação de Ácido Nucleico
Fenótipo
Valor Preditivo dos Testes
Rifampina/farmacologia
Sensibilidade e Especificidade
Escarro/microbiologia
Teste Tuberculínico
Tuberculose/tratamento farmacológico
Tuberculose/epidemiologia
Tuberculose Resistente a Múltiplos Medicamentos/diagnóstico
Tuberculose Resistente a Múltiplos Medicamentos/tratamento farmacológico
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antitubercular Agents); 0 (Bacterial Proteins); 0 (DNA, Bacterial); 0 (Diarylquinolines); 78846I289Y (bedaquiline); EC 3.6.1.- (ATP synthase subunit C, Mycobacterium tuberculosis); EC 3.6.1.- (Bacterial Proton-Translocating ATPases); VJT6J7R4TR (Rifampin)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:151102
[Lr] Data última revisão:
151102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150715
[St] Status:MEDLINE


  8 / 210 MEDLINE  
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[PMID]:25713065
[Au] Autor:Martin J; Hudson J; Hornung T; Frasch WD
[Ad] Endereço:From the School of Life Sciences, Arizona State University, Tempe, Arizona 85287-4501.
[Ti] Título:Fo-driven Rotation in the ATP Synthase Direction against the Force of F1 ATPase in the FoF1 ATP Synthase.
[So] Source:J Biol Chem;290(17):10717-28, 2015 Apr 24.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Living organisms rely on the FoF1 ATP synthase to maintain the non-equilibrium chemical gradient of ATP to ADP and phosphate that provides the primary energy source for cellular processes. How the Fo motor uses a transmembrane electrochemical ion gradient to create clockwise torque that overcomes F1 ATPase-driven counterclockwise torque at high ATP is a major unresolved question. Using single FoF1 molecules embedded in lipid bilayer nanodiscs, we now report the observation of Fo-dependent rotation of the c10 ring in the ATP synthase (clockwise) direction against the counterclockwise force of ATPase-driven rotation that occurs upon formation of a leash with Fo stator subunit a. Mutational studies indicate that the leash is important for ATP synthase activity and support a mechanism in which residues aGlu-196 and cArg-50 participate in the cytoplasmic proton half-channel to promote leash formation.
[Mh] Termos MeSH primário: ATPases Bacterianas Próton-Translocadoras/química
ATPases Bacterianas Próton-Translocadoras/metabolismo
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/biossíntese
Sequência de Aminoácidos
ATPases Bacterianas Próton-Translocadoras/genética
Escherichia coli/enzimologia
Escherichia coli/genética
Proteínas de Escherichia coli/genética
Modelos Moleculares
Dados de Sequência Molecular
Mutagênese Sítio-Dirigida
Conformação Proteica
Subunidades Proteicas
Rotação
Homologia de Sequência de Aminoácidos
Eletricidade Estática
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Protein Subunits); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Bacterial Proton-Translocating ATPases); EC 3.6.1.- (Escherichia coli Proton-Translocating ATPase)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150226
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.646430


  9 / 210 MEDLINE  
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[PMID]:25377721
[Au] Autor:Guan N; Shin HD; Chen RR; Li J; Liu L; Du G; Chen J
[Ad] Endereço:1] Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, Jiangnan University, Wuxi 214122, China [2] Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, Wuxi 214122, China.
[Ti] Título:Understanding of how Propionibacterium acidipropionici respond to propionic acid stress at the level of proteomics.
[So] Source:Sci Rep;4:6951, 2014 Nov 07.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Propionic acid (PA) is an important platform chemical in the food, agriculture, and pharmaceutical industries and is mainly biosynthesized by propionibacteria. Acid tolerance in PA-producing strains is crucial. In previous work, we investigated the acid tolerance mechanism of Propionibacterium acidipropionici at microenvironmental levels by analyzing physiological changes in the parental strain and three PA-tolerant mutants obtained by genome shuffling. However, the molecular mechanism of PA tolerance in P. acidipropionici remained unclear. Here, we performed a comparative proteomics study of P. acidipropionici CGMCC 1.2230 and the acid-tolerant mutant P. acidipropionici WSH1105; MALDI-TOF/MS identified 24 proteins that significantly differed between the parental and shuffled strains. The differentially expressed proteins were mainly categorized as key components of crucial biological processes and the acid stress response. Quantitative reverse transcriptase polymerase chain reaction (qRT-PCR) was used to confirm differential expression of nine key proteins. Overexpression of the secretory protein glyceraldehyde-3-phosphate dehydrogenase and ATP synthase subunit α in Escherichia coli BL21 improved PA and acetic acid tolerance; overexpression of NADH dehydrogenase and methylmalonyl-CoA epimerase improved PA tolerance. These results provide new insights into the acid tolerance of P. acidipropionici and will facilitate the development of PA production through fermentation by propionibacteria.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Embaralhamento de DNA/métodos
Regulação Bacteriana da Expressão Gênica
Propionatos/metabolismo
Propionibacterium/genética
Proteômica
[Mh] Termos MeSH secundário: Ácido Acético/metabolismo
Adaptação Fisiológica
Proteínas de Bactérias/metabolismo
ATPases Bacterianas Próton-Translocadoras/genética
ATPases Bacterianas Próton-Translocadoras/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Fermentação
Gliceraldeído-3-Fosfato Desidrogenase (Fosforiladora)/genética
Gliceraldeído-3-Fosfato Desidrogenase (Fosforiladora)/metabolismo
NADH Desidrogenase/genética
NADH Desidrogenase/metabolismo
Propionibacterium/metabolismo
Racemases e Epimerases/genética
Racemases e Epimerases/metabolismo
Estresse Fisiológico
Transgenes
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Escherichia coli Proteins); 0 (Propionates); EC 1.2.1.12 (Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)); EC 1.6.99.3 (NADH Dehydrogenase); EC 3.6.1.- (Bacterial Proton-Translocating ATPases); EC 3.6.3.14 (atpB protein, E coli); EC 5.1.- (Racemases and Epimerases); EC 5.1.99.1 (methylmalonyl-coenzyme A racemase); JHU490RVYR (propionic acid); Q40Q9N063P (Acetic Acid)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141108
[St] Status:MEDLINE
[do] DOI:10.1038/srep06951


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[PMID]:25203970
[Au] Autor:Worley MV; Estrada SJ
[Ad] Endereço:Department of Pharmacy, Lee Memorial Health System, Fort Myers, Florida.
[Ti] Título:Bedaquiline: a novel antitubercular agent for the treatment of multidrug-resistant tuberculosis.
[So] Source:Pharmacotherapy;34(11):1187-97, 2014 Nov.
[Is] ISSN:1875-9114
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bedaquiline is a diarylquinoline antitubercular drug with a novel mechanism of action against Mycobacterium tuberculosis. Bedaquiline works by inhibiting bacterial adenosine triphosphate (ATP) synthase and represents the first novel class of antituberculosis agents in more than 40 years. Bedaquiline is indicated for the treatment of multidrug-resistant tuberculosis (MDR TB) in combination with at least three other antitubercular drugs when no other effective regimen is available. The recommended bedaquiline dosage is 400 mg orally once/day for 2 weeks followed by 200 mg orally 3 times/week for 22 weeks. Bedaquiline should be administered with food, which increases the bioavailability 2-fold. Bedaquiline is metabolized by cytochrome P450 isoenzyme 3A4 and is impacted by both inducers and inhibitors of this isoenzyme. Concentration-dependent bactericidal activity was observed in laboratory and murine studies. Accelerated approval was granted in the United States and European Union based on the results of two phase IIb clinical studies that used sputum culture clearance as a surrogate end point for clinical efficacy. These studies showed greater sputum culture clearance up to week 24 for the bedaquiline group compared with placebo. Common adverse events in clinical trials included nausea, arthralgia, and headache. Serious adverse events included elevated serum transaminase levels and rate-corrected QT-interval prolongation. Unexplained higher mortality was seen in patients receiving bedaquiline versus those receiving placebo. Bedaquiline is a novel agent with a unique mechanism of action and has the potential to meet a great need in patients with MDR TB who have no other treatment options. Due to safety concerns and limited clinical information, phase III trials are needed to fully determine its place in therapy.
[Mh] Termos MeSH primário: Complexos de ATP Sintetase/antagonistas & inibidores
Antituberculosos/uso terapêutico
Proteínas de Bactérias/antagonistas & inibidores
Diarilquinolinas/uso terapêutico
Inibidores Enzimáticos/uso terapêutico
Mycobacterium tuberculosis/efeitos dos fármacos
Tuberculose Resistente a Múltiplos Medicamentos/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Antituberculosos/efeitos adversos
Antituberculosos/farmacocinética
Antituberculosos/farmacologia
ATPases Bacterianas Próton-Translocadoras
Diarilquinolinas/efeitos adversos
Diarilquinolinas/farmacocinética
Diarilquinolinas/farmacologia
Interações Medicamentosas
Drogas em Investigação/efeitos adversos
Drogas em Investigação/farmacocinética
Drogas em Investigação/farmacologia
Drogas em Investigação/uso terapêutico
Inibidores Enzimáticos/efeitos adversos
Inibidores Enzimáticos/farmacocinética
Inibidores Enzimáticos/farmacologia
Seres Humanos
Mycobacterium tuberculosis/enzimologia
Mycobacterium tuberculosis/crescimento & desenvolvimento
Guias de Prática Clínica como Assunto
Tuberculose Resistente a Múltiplos Medicamentos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antitubercular Agents); 0 (Bacterial Proteins); 0 (Diarylquinolines); 0 (Drugs, Investigational); 0 (Enzyme Inhibitors); 78846I289Y (bedaquiline); EC 2.7.4.- (ATP Synthetase Complexes); EC 3.6.1.- (ATP synthase subunit C, Mycobacterium tuberculosis); EC 3.6.1.- (Bacterial Proton-Translocating ATPases)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140910
[St] Status:MEDLINE
[do] DOI:10.1002/phar.1482



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