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  1 / 10441 MEDLINE  
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[PMID]:29339722
[Au] Autor:Sousa DZ; Visser M; van Gelder AH; Boeren S; Pieterse MM; Pinkse MWH; Verhaert PDEM; Vogt C; Franke S; Kümmel S; Stams AJM
[Ad] Endereço:Laboratory of Microbiology, Wageningen University & Research, Stippeneng 4, 6708 WE, Wageningen, The Netherlands.
[Ti] Título:The deep-subsurface sulfate reducer Desulfotomaculum kuznetsovii employs two methanol-degrading pathways.
[So] Source:Nat Commun;9(1):239, 2018 01 16.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Methanol is generally metabolized through a pathway initiated by a cobalamine-containing methanol methyltransferase by anaerobic methylotrophs (such as methanogens and acetogens), or through oxidation to formaldehyde using a methanol dehydrogenase by aerobes. Methanol is an important substrate in deep-subsurface environments, where thermophilic sulfate-reducing bacteria of the genus Desulfotomaculum have key roles. Here, we study the methanol metabolism of Desulfotomaculum kuznetsovii strain 17 , isolated from a 3000-m deep geothermal water reservoir. We use proteomics to analyze cells grown with methanol and sulfate in the presence and absence of cobalt and vitamin B12. The results indicate the presence of two methanol-degrading pathways in D. kuznetsovii, a cobalt-dependent methanol methyltransferase and a cobalt-independent methanol dehydrogenase, which is further confirmed by stable isotope fractionation. This is the first report of a microorganism utilizing two distinct methanol conversion pathways. We hypothesize that this gives D. kuznetsovii a competitive advantage in its natural environment.
[Mh] Termos MeSH primário: Álcool Desidrogenase/metabolismo
Proteínas de Bactérias/metabolismo
Desulfotomaculum/enzimologia
Redes e Vias Metabólicas/genética
Metanol/metabolismo
Metiltransferases/metabolismo
[Mh] Termos MeSH secundário: Álcool Desidrogenase/genética
Proteínas de Bactérias/genética
Cobalto/metabolismo
Cobalto/farmacologia
Meios de Cultura/química
Desulfotomaculum/genética
Expressão Gênica
Perfilação da Expressão Gênica
Hidrólise
Metiltransferases/genética
Oxirredução
Filogenia
Proteômica/métodos
Vitamina B 12/metabolismo
Vitamina B 12/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Culture Media); 3G0H8C9362 (Cobalt); EC 1.1.1.1 (Alcohol Dehydrogenase); EC 2.1.1.- (Methyltransferases); EVS87XF13W (cobaltous chloride); P6YC3EG204 (Vitamin B 12); Y4S76JWI15 (Methanol)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02518-9


  2 / 10441 MEDLINE  
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[PMID]:29317652
[Au] Autor:Santos-Barriopedro I; Bosch-Presegué L; Marazuela-Duque A; de la Torre C; Colomer C; Vazquez BN; Fuhrmann T; Martínez-Pastor B; Lu W; Braun T; Bober E; Jenuwein T; Serrano L; Esteller M; Chen Z; Barceló-Batllori S; Mostoslavsky R; Espinosa L; Vaquero A
[Ad] Endereço:Chromatin Biology Laboratory, Cancer Epigenetics and Biology Program (PEBC), Bellvitge Biomedical Research Institute (IDIBELL), Av. Gran Via de l'Hospitalet 199-203, 08908, L'Hospitalet de Llobregat (Barcelona), Spain.
[Ti] Título:SIRT6-dependent cysteine monoubiquitination in the PRE-SET domain of Suv39h1 regulates the NF-κB pathway.
[So] Source:Nat Commun;9(1):101, 2018 01 09.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Sirtuins are NAD -dependent deacetylases that facilitate cellular stress response. They include SirT6, which protects genome stability and regulates metabolic homeostasis through gene silencing, and whose loss induces an accelerated aging phenotype directly linked to hyperactivation of the NF-κB pathway. Here we show that SirT6 binds to the H3K9me3-specific histone methyltransferase Suv39h1 and induces monoubiquitination of conserved cysteines in the PRE-SET domain of Suv39h1. Following activation of NF-κB signaling Suv39h1 is released from the IκBα locus, subsequently repressing the NF-κB pathway. We propose that SirT6 attenuates the NF-κB pathway through IκBα upregulation via cysteine monoubiquitination and chromatin eviction of Suv39h1. We suggest a mechanism based on SirT6-mediated enhancement of a negative feedback loop that restricts the NF-κB pathway.
[Mh] Termos MeSH primário: Cisteína/metabolismo
Metiltransferases/metabolismo
NF-kappa B/metabolismo
Domínios PR-SET
Proteínas Repressoras/metabolismo
Sirtuínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Células Cultivadas
Cromatina/metabolismo
Cisteína/genética
Células HCT116
Células HEK293
Células HeLa
Seres Humanos
Metiltransferases/genética
Camundongos
Inibidor de NF-kappaB alfa/metabolismo
Células NIH 3T3
Ligação Proteica
Proteínas Repressoras/genética
Transdução de Sinais
Sirtuínas/genética
Ubiquitinação
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin); 0 (NF-kappa B); 0 (Repressor Proteins); 139874-52-5 (NF-KappaB Inhibitor alpha); EC 2.1.1. (SUV39H1 protein, human); EC 2.1.1.- (Methyltransferases); EC 3.5.1.- (SIRT6 protein, human); EC 3.5.1.- (Sirtuins); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02586-x


  3 / 10441 MEDLINE  
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[PMID]:29199993
[Au] Autor:Pampa KJ; Madan Kumar S; Hema MK; Kumara K; Naveen S; Kunishima N; Lokanath NK
[Ad] Endereço:Department of Studies in Biotechnology, University of Mysore, Manasagangotri, Mysuru, Karnataka 570 006, India.
[Ti] Título:Crystal structure of SAM-dependent methyltransferase from Pyrococcus horikoshii.
[So] Source:Acta Crystallogr F Struct Biol Commun;73(Pt 12):706-712, 2017 Dec 01.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Methyltransferases (MTs) are enzymes involved in methylation that are needed to perform cellular processes such as biosynthesis, metabolism, gene expression, protein trafficking and signal transduction. The cofactor S-adenosyl-L-methionine (SAM) is used for catalysis by SAM-dependent methyltransferases (SAM-MTs). The crystal structure of Pyrococcus horikoshii SAM-MT was determined to a resolution of 2.1 Šusing X-ray diffraction. The monomeric structure consists of a Rossmann-like fold (domain I) and a substrate-binding domain (domain II). The cofactor (SAM) molecule binds at the interface between adjacent subunits, presumably near to the active site(s) of the enzyme. The observed dimeric state might be important for the catalytic function of the enzyme.
[Mh] Termos MeSH primário: Metiltransferases/química
Metiltransferases/metabolismo
Pyrococcus horikoshii/enzimologia
S-Adenosilmetionina/metabolismo
[Mh] Termos MeSH secundário: Proteínas Arqueais/química
Proteínas Arqueais/metabolismo
Sítios de Ligação
Cristalografia por Raios X
Modelos Moleculares
Conformação Proteica
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 7LP2MPO46S (S-Adenosylmethionine); EC 2.1.1.- (Methyltransferases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X17016648


  4 / 10441 MEDLINE  
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[PMID]:28471404
[Au] Autor:Aubee JI; Olu M; Thompson KM
[Ad] Endereço:Department of Microbiology, College of Medicine, Howard University, Washington, DC 20059, USA. joseph.aubee@howard.edu.
[Ti] Título:TrmL and TusA Are Necessary for rpoS and MiaA Is Required for hfq Expression in Escherichia coli.
[So] Source:Biomolecules;7(2), 2017 May 04.
[Is] ISSN:2218-273X
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Previous work demonstrated that efficient RNA Polymerase sigma S-subunit (RpoS) translation requires the N6-isopentenyladenosine i6A37 transfer RNA (tRNA) modification for UUX-Leu decoding. Here we investigate the effect of two additional tRNA modification systems on RpoS translation; the analysis was also extended to another High UUX-leucine codon (HULC) protein, Host Factor for phage Qß (Hfq). One tRNA modification, the addition of the 2'-O-methylcytidine/uridine 34 (C/U34m) tRNA modification by tRNA (cytidine/uridine-2'O)-ribose methyltransferase L (TrmL), requires the presence of the 6-isopentenyladenosine 37 (i6A37) and therefore it seemed possible that the defect in RpoS translation in the absence of i6A37 prenyl transferase (MiaA) was in fact due to the inability to add the C/U34m modification to UUX-Leu tRNAs. The second modification, addition of 2-thiouridine (s²U), part of (mnm5s²U34), is dependent on tRNA 2-thiouridine synthesizing protein A (TusA), previously shown to affect RpoS levels. We compared expression of P - translational fusions carrying wild-type UUX leucine codons with derivatives in which UUX codons were changed to CUX codons, in the presence and absence of TrmL or TusA. The absence of these proteins, and therefore presumably the modifications they catalyze, both abolished P - - translation activity. UUX-Leu to CUX-Leu codon mutations in suppressed the requirement for P - - expression. Thus, it is likely that the C/U34m and s²U34 tRNA modifications are necessary for full translation. We also measured P - translational fusion activity in the absence of C/U34m ( ) or i6A37 ( ). The absence of i6A37 resulted in decreased P - expression, consistent with a role for i6A37 tRNA modification for translation.
[Mh] Termos MeSH primário: Alquil e Aril Transferases/metabolismo
Proteínas de Bactérias/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Escherichia coli/metabolismo
Regulação Bacteriana da Expressão Gênica
Fator Proteico 1 do Hospedeiro/genética
Metiltransferases/metabolismo
Fator sigma/metabolismo
[Mh] Termos MeSH secundário: Sequência de Bases
Escherichia coli/genética
RNA de Transferência/genética
RNA de Transferência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Escherichia coli Proteins); 0 (Hfq protein, E coli); 0 (Host Factor 1 Protein); 0 (Sigma Factor); 0 (TusA protein, E coli); 0 (sigma factor KatF protein, Bacteria); 9014-25-9 (RNA, Transfer); EC 2.1.1.- (Methyltransferases); EC 2.1.1.- (TrmL protein, E coli); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.27 (adenylate isopentenyltransferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180219
[Lr] Data última revisão:
180219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


  5 / 10441 MEDLINE  
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[PMID]:29343685
[Au] Autor:Zhu B; Chen S; Wang H; Yin C; Han C; Peng C; Liu Z; Wan L; Zhang X; Zhang J; Lian CG; Ma P; Xu ZX; Prince S; Wang T; Gao X; Shi Y; Liu D; Liu M; Wei W; Wei Z; Pan J; Wang Y; Xuan Z; Hess J; Hayward NK; Goding CR; Chen X; Zhou J; Cui R
[Ad] Endereço:Department of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA, 02118, USA.
[Ti] Título:The protective role of DOT1L in UV-induced melanomagenesis.
[So] Source:Nat Commun;9(1):259, 2018 01 17.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The DOT1L histone H3 lysine 79 (H3K79) methyltransferase plays an oncogenic role in MLL-rearranged leukemogenesis. Here, we demonstrate that, in contrast to MLL-rearranged leukemia, DOT1L plays a protective role in ultraviolet radiation (UVR)-induced melanoma development. Specifically, the DOT1L gene is located in a frequently deleted region and undergoes somatic mutation in human melanoma. Specific mutations functionally compromise DOT1L methyltransferase enzyme activity leading to reduced H3K79 methylation. Importantly, in the absence of DOT1L, UVR-induced DNA damage is inefficiently repaired, so that DOT1L loss promotes melanoma development in mice after exposure to UVR. Mechanistically, DOT1L facilitates DNA damage repair, with DOT1L-methylated H3K79 involvement in binding and recruiting XPC to the DNA damage site for nucleotide excision repair (NER). This study indicates that DOT1L plays a protective role in UVR-induced melanomagenesis.
[Mh] Termos MeSH primário: Melanoma/etiologia
Metiltransferases/genética
[Mh] Termos MeSH secundário: Animais
Carcinogênese
Células Cultivadas
Reparo do DNA
Proteínas de Ligação a DNA/metabolismo
Seres Humanos
Mutação com Perda de Função
Melanoma/metabolismo
Metiltransferases/metabolismo
Camundongos
Camundongos Knockout
Proteínas Proto-Oncogênicas B-raf/genética
Raios Ultravioleta
[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 (DNA-Binding Proteins); 156533-34-5 (XPC protein, human); EC 2.1.1.- (DOT1L protein, human); EC 2.1.1.- (Dot1l protein, mouse); EC 2.1.1.- (Methyltransferases); EC 2.7.11.1 (BRAF protein, human); EC 2.7.11.1 (Proto-Oncogene Proteins B-raf)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180119
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02687-7


  6 / 10441 MEDLINE  
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[PMID]:29198372
[Au] Autor:Mancini S; Poirel L; Corthesy M; Greub G; Nordmann P
[Ad] Endereço:Emerging Antibiotic Resistance Unit, Medical and Molecular Microbiology, Department of Medicine, University of Fribourg, Fribourg, Switzerland; French INSERM European Unit, University of Fribourg (LEA-IAME), Fribourg, Switzerland; Swiss National Reference Center for Emerging Antibiotic Resistance, F
[Ti] Título:Klebsiella pneumoniae co-producing KPC and RmtG, finally targeting Switzerland.
[So] Source:Diagn Microbiol Infect Dis;90(2):151-152, 2018 Feb.
[Is] ISSN:1879-0070
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A carbapenem- and pan-aminoglycoside-resistant Klebsiella pneumoniae strain was isolated from a Brazilian patient hospitalized in a Swiss hospital. The clinical isolate carried genes encoding the KPC-2 carbapenemase and the RmtG 16S rRNA methyltransferase. This is the first report of a carbapenem-resistant K. pneumoniae producing RmtG in Europe.
[Mh] Termos MeSH primário: Infecção Hospitalar/microbiologia
Farmacorresistência Bacteriana Múltipla/genética
Infecções por Klebsiella/microbiologia
Klebsiella pneumoniae/genética
[Mh] Termos MeSH secundário: Idoso
Antibacterianos/farmacologia
Proteínas de Bactérias/genética
Brasil
Infecção Hospitalar/epidemiologia
Surtos de Doenças
Seres Humanos
Klebsiella pneumoniae/efeitos dos fármacos
Klebsiella pneumoniae/enzimologia
Metiltransferases/genética
Testes de Sensibilidade Microbiana
Suíça
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); EC 2.1.1.- (Methyltransferases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE


  7 / 10441 MEDLINE  
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[PMID]:29326266
[Au] Autor:Pace L; Goudot C; Zueva E; Gueguen P; Burgdorf N; Waterfall JJ; Quivy JP; Almouzni G; Amigorena S
[Ad] Endereço:Institut Curie, PSL Research University, F-75005 Paris, France. luigia.pace@iigm.it genevieve.almouzni@curie.fr sebastian.amigorena@curie.fr.
[Ti] Título:The epigenetic control of stemness in CD8 T cell fate commitment.
[So] Source:Science;359(6372):177-186, 2018 Jan 12.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:After priming, naïve CD8 T lymphocytes establish specific heritable transcription programs that define progression to long-lasting memory cells or to short-lived effector cells. Although lineage specification is critical for protection, it remains unclear how chromatin dynamics contributes to the control of gene expression programs. We explored the role of gene silencing by the histone methyltransferase Suv39h1. In murine CD8 T cells activated after infection, Suv39h1-dependent trimethylation of histone H3 lysine 9 controls the expression of a set of stem cell-related memory genes. Single-cell RNA sequencing revealed a defect in silencing of stem/memory genes selectively in -defective T cell effectors. As a result, -defective CD8 T cells show sustained survival and increased long-term memory reprogramming capacity. Thus, Suv39h1 plays a critical role in marking chromatin to silence stem/memory genes during CD8 T effector terminal differentiation.
[Mh] Termos MeSH primário: Linfócitos T CD8-Positivos/imunologia
Linfócitos T CD8-Positivos/metabolismo
Inativação Gênica
Histona-Lisina N-Metiltransferase/metabolismo
Memória Imunológica
Listeriose/imunologia
Metiltransferases/metabolismo
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular
Células Cultivadas
Cromatina/metabolismo
Epigênese Genética
Feminino
Histona-Lisina N-Metiltransferase/genética
Histonas/metabolismo
Listeria monocytogenes/imunologia
Masculino
Metilação
Metiltransferases/genética
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Proteínas Repressoras/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (Histones); 0 (RNA, Messenger); 0 (Repressor Proteins); EC 2.1.1. (Suv39h1 protein, mouse); EC 2.1.1.- (Methyltransferases); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE
[do] DOI:10.1126/science.aah6499


  8 / 10441 MEDLINE  
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[PMID]:29298302
[Au] Autor:Züst R; Li SH; Xie X; Velumani S; Chng M; Toh YX; Zou J; Dong H; Shan C; Pang J; Qin CF; Newell EW; Shi PY; Fink K
[Ad] Endereço:Singapore Immunology Network, Agency for Science, Technology and Research, Singapore, Singapore.
[Ti] Título:Characterization of a candidate tetravalent vaccine based on 2'-O-methyltransferase mutants.
[So] Source:PLoS One;13(1):e0189262, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dengue virus (DENV) is one of the most widespread arboviruses. The four DENV serotypes infect about 400 million people every year, causing 96 million clinical dengue cases, of which approximately 500'000 are severe and potentially life-threatening. The only licensed vaccine has a limited efficacy and is only recommended in regions with high endemicity. We previously reported that 2'-O-methyltransferase mutations in DENV-1 and DENV-2 block their capacity to inhibit type I IFNs and render the viruses attenuated in vivo, making them amenable as vaccine strains; here we apply this strategy to all four DENV serotypes to generate a tetravalent, non-chimeric live-attenuated dengue vaccine. 2'-O-methyltransferase mutants of all four serotypes are highly sensitive to type I IFN inhibition in human cells. The tetravalent formulation is attenuated and immunogenic in mice and cynomolgus macaques and elicits a response that protects from virus challenge. These results show the potential of 2'-O-methyltransferase mutant viruses as a safe, tetravalent, non-chimeric dengue vaccine.
[Mh] Termos MeSH primário: Vacinas contra Dengue/imunologia
Vírus da Dengue/imunologia
Metiltransferases/genética
Mutação
[Mh] Termos MeSH secundário: Animais
Anticorpos Neutralizantes/análise
Anticorpos Neutralizantes/imunologia
Linhagem Celular
Ensaio de Imunoadsorção Enzimática
Feminino
Seres Humanos
Macaca fascicularis
Masculino
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Dengue Vaccines); EC 2.1.1.- (Methyltransferases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180206
[Lr] Data última revisão:
180206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180104
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189262


  9 / 10441 MEDLINE  
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[PMID]:27771305
[Au] Autor:Walter ME; Ortiz A; Sondgeroth C; Sindt NM; Duszenko N; Catlett JL; Zhou Y; Valloppilly S; Anderson C; Fernando S; Buan NR
[Ad] Endereço:Redox Biology Center, Department of Biochemistry, University of Nebraska-Lincoln, N200 Beadle Center, Lincoln, NE 68588-0664, United States.
[Ti] Título:High-throughput mutation, selection, and phenotype screening of mutant methanogenic archaea.
[So] Source:J Microbiol Methods;131:113-121, 2016 12.
[Is] ISSN:1872-8359
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Bacterial and archaeal genomes can contain 30% or more hypothetical genes with no predicted function. Phylogenetically deep-branching microbes, such as methane-producing archaea (methanogens), contain up to 50% genes with unknown function. In order to formulate hypotheses about the function of hypothetical gene functions in the strict anaerobe, Methanosarcina acetivorans, we have developed high-throughput anaerobic techniques to UV mutagenize, screen, and select for mutant strains in 96-well plates. Using these approaches we have isolated 10 mutant strains that exhibit a variety of physiological changes including increased or decreased growth rate relative to the parent strain when cells use methanol and/or acetate as carbon and energy sources. This method provides an avenue for the first step in identifying new gene functions: associating a genetic mutation with a reproducible phenotype. Mutations in bona fide methanogenesis genes such as corrinoid methyltransferases and proton-translocating F H :methanophenazine oxidoreductase (Fpo) were also generated, opening the door to in vivo functional complementation experiments. Irradiation-based mutagenesis such as from ultraviolet (UV) light, combined with modern genome sequencing, is a useful procedure to discern systems-level gene function in prokaryote taxa that can be axenically cultured but which may be resistant to chemical mutagens.
[Mh] Termos MeSH primário: Archaea/genética
Archaea/isolamento & purificação
Archaea/efeitos da radiação
Ensaios de Triagem em Larga Escala/métodos
Fenótipo
Mutação Puntual/efeitos da radiação
Raios Ultravioleta
[Mh] Termos MeSH secundário: Acetatos/metabolismo
Archaea/metabolismo
DNA Arqueal/genética
DNA Arqueal/efeitos da radiação
Genes Arqueais
Metano/metabolismo
Metanol/metabolismo
Methanosarcina/genética
Methanosarcina/crescimento & desenvolvimento
Methanosarcina/efeitos da radiação
Metiltransferases/genética
Viabilidade Microbiana/efeitos da radiação
Mutagênese/efeitos da radiação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acetates); 0 (DNA, Archaeal); EC 2.1.1.- (Methyltransferases); OP0UW79H66 (Methane); Y4S76JWI15 (Methanol)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180126
[Lr] Data última revisão:
180126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161107
[St] Status:MEDLINE


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[PMID]:28455137
[Au] Autor:Ben Mouhoub R; El May A; Cheraief I; Landoulsi A
[Ad] Endereço:Biochemistry and Molecular Biology, Code UR13ES34 Research Unit, Faculty of Sciences of Bizerte, Zarzouna 7021, Carthage University, Tunisia. Electronic address: ramlabenmouhoub@gmail.com.
[Ti] Título:Influence of static magnetic field exposure on fatty acid composition in Salmonella Hadar.
[So] Source:Microb Pathog;108:13-20, 2017 Jul.
[Is] ISSN:1096-1208
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We have been interested, in this work, to investigate the effect of the exposure to static magnetic field at 200 mT (SMF) on the fatty acid (FA) composition of Salmonella enterica subsp Enterica serovar Hadar isolate 287: effects on the proportion of saturated and unsaturated fatty acids (SFAs, UFAs), cyclopropane fatty acids (CFAs) and hydroxy fatty acids after exposure to the static magnetic field at 200 mT (SMF). Analysis with Gas Chromatography-Mass Spectrometry (GC-MS) of total lipid showed that the proportion of the most fatty acids was clearly affected. The comparison of UFAs/SFAs ratio in exposed bacteria and controls showed a diminution after 3 and 6 h of exposure. This ration reached a balance after 9 h of treatment with SMF. So we can conclude that S. Hadar tries to adapt to magnetic stress by changing the proportions of SFAs and UFAs over time to maintain an equilibrium after 9 h of exposure, thus to maintain the inner membranes fluidity. Also, a decrease in the proportion of hydroxy FAs was observed after 6 h but an increase of this proportion after 9 h of exposure. Concerning CFAs, its proportion raised after 6 h of exposure to the SMF but it decreased after 9 h of exposure. These results are strongly correlated with those of cfa (cyclopropane fatty acid synthase) gene expression which showed a decrease of its expression after 9 h of exposure.
[Mh] Termos MeSH primário: Ácidos Graxos/análise
Campos Magnéticos
Salmonella enterica/metabolismo
Salmonella enterica/efeitos da radiação
[Mh] Termos MeSH secundário: Ciclopropanos/análise
Ciclopropanos/química
Ácidos Graxos/química
Ácidos Graxos/genética
Ácidos Graxos Insaturados/análise
Ácidos Graxos Insaturados/química
Ácidos Graxos Insaturados/genética
Cromatografia Gasosa-Espectrometria de Massas
Regulação Bacteriana da Expressão Gênica/efeitos da radiação
Fluidez de Membrana/efeitos da radiação
Lipídeos de Membrana
Metiltransferases/genética
Metiltransferases/efeitos da radiação
RNA Bacteriano/análise
RNA Ribossômico 16S/genética
Salmonella enterica/genética
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyclopropanes); 0 (Fatty Acids); 0 (Fatty Acids, Unsaturated); 0 (Membrane Lipids); 0 (RNA, Bacterial); 0 (RNA, Ribosomal, 16S); 0 (cyclopropane fatty acids); EC 2.1.1.- (Methyltransferases); EC 2.1.1.- (cyclopropane synthetase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE



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