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Pesquisa : G02.111.012.052 [Categoria DeCS]
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  1 / 18716 MEDLINE  
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[PMID]:27777629
[Au] Autor:Lau AC; Zhu KP; Brouhard EA; Davis MB; Csankovszki G
[Ad] Endereço:Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N. University Ave., Ann Arbor, MI 48109-1048 USA ; Genome Technologies, The Jackson Laboratory for Genomic Medicine, Farmington, CT 06032 USA.
[Ti] Título:An H4K16 histone acetyltransferase mediates decondensation of the X chromosome in males.
[So] Source:Epigenetics Chromatin;9:44, 2016.
[Is] ISSN:1756-8935
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: In , in order to equalize gene expression between the sexes and balance X and autosomal expression, two steps are believed to be required. First, an unknown mechanism is hypothesized to upregulate the X chromosome in both sexes. This mechanism balances the X to autosomal expression in males, but creates X overexpression in hermaphrodites. Therefore, to restore the balance, hermaphrodites downregulate gene expression twofold on both X chromosomes. While many studies have focused on X chromosome downregulation, the mechanism of X upregulation is not known. RESULTS: To gain more insight into X upregulation, we studied the effects of chromatin condensation and histone acetylation on gene expression levels in male . We have found that the H4K16 histone acetyltransferase MYS-1/Tip60 mediates dramatic decondensation of the male X chromosome as measured by FISH. However, RNA-seq analysis revealed that MYS-1 contributes only slightly to upregulation of gene expression on the X chromosome. These results suggest that the level of chromosome decondensation does not necessarily correlate with the degree of gene expression change in vivo. Furthermore, the X chromosome is more sensitive to MYS-1-mediated decondensation than the autosomes, despite similar levels of H4K16ac on all chromosomes, as measured by ChIP-seq. H4K16ac levels weakly correlate with gene expression levels on both the X and the autosomes, but highly expressed genes on the X chromosome do not contain exceptionally high levels of H4K16ac. CONCLUSION: These results indicate that H4K16ac and chromosome decondensation influence regulation of the male X chromosome; however, they do not fully account for the high levels of gene expression observed on the X chromosomes.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/metabolismo
Histona Acetiltransferases/metabolismo
Cromossomo X/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Animais
Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/genética
Cromatina/metabolismo
Montagem e Desmontagem da Cromatina
Imunoprecipitação da Cromatina
Compensação de Dosagem (Genética)
Expressão Gênica
Histona Acetiltransferases/genética
Histonas/metabolismo
Hibridização in Situ Fluorescente
Masculino
Análise de Sequência de DNA
Cromossomo X/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Chromatin); 0 (Histones); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (MYS-1 protein, C elegans)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180310
[Lr] Data última revisão:
180310
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


  2 / 18716 MEDLINE  
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[PMID]:28471062
[Au] Autor:Rao AN; Patil A; Brodnik ZD; Qiang L; España RA; Sullivan KA; Black MM; Baas PW
[Ad] Endereço:Department of Neurobiology and Anatomy, Drexel University College of Medicine, Philadelphia, Pennsylvania.
[Ti] Título:Pharmacologically increasing microtubule acetylation corrects stress-exacerbated effects of organophosphates on neurons.
[So] Source:Traffic;18(7):433-441, 2017 Jul.
[Is] ISSN:1600-0854
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Many veterans of the 1990-1991 Gulf War contracted Gulf War Illness (GWI), a multisymptom disease that primarily affects the nervous system. Here, we treated cultures of human or rat neurons with diisopropyl fluorophosphate (DFP), an analog of sarin, one of the organophosphate (OP) toxicants to which the military veterans were exposed. All observed cellular defects produced by DFP were exacerbated by pretreatment with corticosterone or cortisol, which, in rat and human neurons, respectively, serves in our experiments to mimic the physical stress endured by soldiers during the war. To best mimic the disease, DFP was used below the level needed to inhibit acetylcholinesterase. We observed a diminution in the ratio of acetylated to total tubulin that was correctable by treatment with tubacin, a drug that inhibits HDAC6, the tubulin deacetylase. The reduction in microtubule acetylation was coupled with deficits in microtubule dynamics, which were correctable by HDAC6 inhibition. Deficits in mitochondrial transport and dopamine release were also improved by tubacin. Thus, various negative effects of the toxicant/stress exposures were at least partially correctable by restoring microtubule acetylation to a more normal status. Such an approach may have therapeutic benefit for individuals suffering from GWI or other neurological disorders linked to OP exposure.
[Mh] Termos MeSH primário: Anilidas/farmacologia
Substâncias para a Guerra Química/toxicidade
Ácidos Hidroxâmicos/farmacologia
Isoflurofato/toxicidade
Microtúbulos/efeitos dos fármacos
Neurônios/efeitos dos fármacos
Estresse Fisiológico
[Mh] Termos MeSH secundário: Acetilação
Animais
Transporte Biológico
Células Cultivadas
Corticosterona/farmacologia
Dopamina/secreção
Relação Dose-Resposta a Droga
Seres Humanos
Hidrocortisona/farmacologia
Microtúbulos/metabolismo
Mitocôndrias/efeitos dos fármacos
Mitocôndrias/metabolismo
Síndrome do Golfo Pérsico
Ratos
Tubulina (Proteína)/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anilides); 0 (Chemical Warfare Agents); 0 (Hydroxamic Acids); 0 (Tubulin); 02C2G1D30D (tubacin); 12UHW9R67N (Isoflurophate); VTD58H1Z2X (Dopamine); W980KJ009P (Corticosterone); WI4X0X7BPJ (Hydrocortisone)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1111/tra.12489


  3 / 18716 MEDLINE  
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[PMID]:28462789
[Au] Autor:Ren J; Sang Y; Lu J; Yao YF
[Ad] Endereço:Laboratory of Bacterial Pathogenesis, Department of Microbiology and Immunology, Institutes of Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.
[Ti] Título:Protein Acetylation and Its Role in Bacterial Virulence.
[So] Source:Trends Microbiol;25(9):768-779, 2017 Sep.
[Is] ISSN:1878-4380
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Protein acetylation is a universal post-translational modification which is found in both eukaryotes and prokaryotes. This process is achieved enzymatically by the protein acetyltransferase Pat, and nonenzymatically by metabolic intermediates (e.g., acetyl phosphate) in bacteria. Protein acetylation plays a role in bacterial chemotaxis, metabolism, DNA replication, and other cellular processes. Recently, accumulating evidence has suggested that protein acetylation might be involved in bacterial virulence because a number of bacterial virulence factors are acetylated. In this review, we summarize the progress in understanding bacterial protein acetylation and discuss how it mediates bacterial virulence.
[Mh] Termos MeSH primário: Acetiltransferases/metabolismo
Bactérias/metabolismo
Bactérias/patogenicidade
Proteínas/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Bactérias/enzimologia
Proteínas de Bactérias/metabolismo
Carbono/metabolismo
Nitrogênio/metabolismo
Processamento de Proteína Pós-Traducional
Proteômica
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Proteins); 7440-44-0 (Carbon); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (protein acyltransferase); N762921K75 (Nitrogen)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


  4 / 18716 MEDLINE  
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[PMID]:28460463
[Au] Autor:Almeida LO; Neto MPC; Sousa LO; Tannous MA; Curti C; Leopoldino AM
[Ad] Endereço:Department of Clinical Analyses, Toxicology and Food Sciences, School of Pharmaceutical Sciences of Ribeirão Preto, University of São Paulo, Ribeirão Preto, SP, Brazil.
[Ti] Título:SET oncoprotein accumulation regulates transcription through DNA demethylation and histone hypoacetylation.
[So] Source:Oncotarget;8(16):26802-26818, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Epigenetic modifications are essential in the control of normal cellular processes and cancer development. DNA methylation and histone acetylation are major epigenetic modifications involved in gene transcription and abnormal events driving the oncogenic process. SET protein accumulates in many cancer types, including head and neck squamous cell carcinoma (HNSCC); SET is a member of the INHAT complex that inhibits gene transcription associating with histones and preventing their acetylation. We explored how SET protein accumulation impacts on the regulation of gene expression, focusing on DNA methylation and histone acetylation. DNA methylation profile of 24 tumour suppressors evidenced that SET accumulation decreased DNA methylation in association with loss of 5-methylcytidine, formation of 5-hydroxymethylcytosine and increased TET1 levels, indicating an active DNA demethylation mechanism. However, the expression of some suppressor genes was lowered in cells with high SET levels, suggesting that loss of methylation is not the main mechanism modulating gene expression. SET accumulation also downregulated the expression of 32 genes of a panel of 84 transcription factors, and SET directly interacted with chromatin at the promoter of the downregulated genes, decreasing histone acetylation. Gene expression analysis after cell treatment with 5-aza-2'-deoxycytidine (5-AZA) and Trichostatin A (TSA) revealed that histone acetylation reversed transcription repression promoted by SET. These results suggest a new function for SET in the regulation of chromatin dynamics. In addition, TSA diminished both SET protein levels and SET capability to bind to gene promoter, suggesting that administration of epigenetic modifier agents could be efficient to reverse SET phenotype in cancer.
[Mh] Termos MeSH primário: Metilação de DNA
Regulação Neoplásica da Expressão Gênica
Chaperonas de Histonas/metabolismo
Histonas/metabolismo
Proteínas Oncogênicas/metabolismo
Fatores de Transcrição/metabolismo
Transcrição Genética
[Mh] Termos MeSH secundário: Acetilação
Carcinoma Pulmonar de Células não Pequenas/genética
Carcinoma Pulmonar de Células não Pequenas/metabolismo
Linhagem Celular Tumoral
Epigênese Genética
Perfilação da Expressão Gênica
Chaperonas de Histonas/genética
Seres Humanos
Modelos Biológicos
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histone Chaperones); 0 (Histones); 0 (Oncogene Proteins); 0 (SET protein, human); 0 (Transcription Factors)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15818


  5 / 18716 MEDLINE  
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[PMID]:29352283
[Au] Autor:Contreras C; Villasana M; Hendzel MJ; Carrero G
[Ad] Endereço:Department of Mathematical and Statistical Sciences, University of Alberta, Edmonton, Alberta, Canada.
[Ti] Título:Using a model comparison approach to describe the assembly pathway for histone H1.
[So] Source:PLoS One;13(1):e0191562, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Histones H1 or linker histones are highly dynamic proteins that diffuse throughout the cell nucleus and associate with chromatin (DNA and associated proteins). This binding interaction of histone H1 with the chromatin is thought to regulate chromatin organization and DNA accessibility to transcription factors and has been proven to involve a kinetic process characterized by a population that associates weakly with chromatin and rapidly dissociates and another population that resides at a binding site for up to several minutes before dissociating. When considering differences between these two classes of interactions in a mathematical model for the purpose of describing and quantifying the dynamics of histone H1, it becomes apparent that there could be several assembly pathways that explain the kinetic data obtained in living cells. In this work, we model these different pathways using systems of reaction-diffusion equations and carry out a model comparison analysis using FRAP (fluorescence recovery after photobleaching) experimental data from different histone H1 variants to determine the most feasible mechanism to explain histone H1 binding to chromatin. The analysis favors four different chromatin assembly pathways for histone H1 which share common features and provide meaningful biological information on histone H1 dynamics. We show, using perturbation analysis, that the explicit consideration of high- and low-affinity associations of histone H1 with chromatin in the favored assembly pathways improves the interpretation of histone H1 experimental FRAP data. To illustrate the results, we use one of the favored models to assess the kinetic changes of histone H1 after core histone hyperacetylation, and conclude that this post-transcriptional modification does not affect significantly the transition of histone H1 from a weakly bound state to a tightly bound state.
[Mh] Termos MeSH primário: Montagem e Desmontagem da Cromatina/fisiologia
Histonas/metabolismo
Modelos Biológicos
[Mh] Termos MeSH secundário: Acetilação
Animais
Cromatina/química
Cromatina/metabolismo
DNA/metabolismo
Recuperação de Fluorescência Após Fotodegradação
Histonas/química
Cinética
Ligação Proteica
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin); 0 (Histones); 9007-49-2 (DNA)
[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:180121
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191562


  6 / 18716 MEDLINE  
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[PMID]:28456748
[Au] Autor:van Gils N; Verhagen HJMP; Smit L
[Ad] Endereço:Department of Hematology, VU University Medical Center, Cancer Center Amsterdam, Amsterdam, The Netherlands.
[Ti] Título:Reprogramming acute myeloid leukemia into sensitivity for retinoic-acid-driven differentiation.
[So] Source:Exp Hematol;52:12-23, 2017 08.
[Is] ISSN:1873-2399
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The success of all-trans retinoic acid (ATRA) therapy for acute promyelocytic leukemia (APL) provides a rationale for using retinoic acid (RA)-based therapy for other subtypes of acute myeloid leukemia (AML). Recently, several studies showed that ATRA may drive leukemic cells efficiently into differentiation and/or apoptosis in a subset of AML patients with an NPM1 mutation, a FLT3-ITD, an IDH1 mutation, and patients overexpressing EVI-1. Because not all patients within these molecular subgroups respond to ATRA and clinical trials that tested ATRA response in non-APL AML patients have had disappointing results, the identification of additional biomarkers may help to identify patients who strongly respond to ATRA-based therapy. Searching for response biomarkers might also reveal novel RA-based combination therapies with an efficient differentiation/apoptosis-inducing effect in non-APL AML patients. Preliminary studies suggest that the epigenetic or transcriptional state of leukemia cells determines their susceptibility to ATRA. We hypothesize that reprogramming by inhibitors of epigenetic-modifying enzymes or by modulation of microRNA expression might sensitize non-APL AML cells for RA-based therapy. AML relapse is caused by a subpopulation of leukemia cells, named leukemic stem cells (LSCs), which are in a different epigenetic state than the total bulk of the AML. The survival of LSCs after therapy is the main cause of the poor prognosis of AML patients, and novel differentiation therapies should drive these LSCs into maturity. In this review, we summarize the current knowledge on the epigenetic aspects of susceptibility to RA-induced differentiation in APL and non-APL AML.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Diferenciação Celular/efeitos dos fármacos
Leucemia Mieloide/tratamento farmacológico
Tretinoína/uso terapêutico
[Mh] Termos MeSH secundário: Acetilação/efeitos dos fármacos
Doença Aguda
Antineoplásicos/uso terapêutico
Apoptose/genética
Diferenciação Celular/genética
Regulação Leucêmica da Expressão Gênica/efeitos dos fármacos
Histonas/metabolismo
Seres Humanos
Leucemia Mieloide/genética
Leucemia Mieloide/patologia
MicroRNAs/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Histones); 0 (MicroRNAs); 5688UTC01R (Tretinoin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180224
[Lr] Data última revisão:
180224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE


  7 / 18716 MEDLINE  
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[PMID]:28450734
[Au] Autor:Woo H; Dam Ha S; Lee SB; Buratowski S; Kim T
[Ad] Endereço:Department of Life Science, Ewha Womans University, Seoul, Korea.
[Ti] Título:Modulation of gene expression dynamics by co-transcriptional histone methylations.
[So] Source:Exp Mol Med;49(4):e326, 2017 04 28.
[Is] ISSN:2092-6413
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Co-transcriptional methylations of histone H3 at lysines 4 and 36, highly conserved methyl marks from yeast to humans, have profound roles in regulation of histone acetylation. These modifications function to recruit and/or activate distinct histone acetyltransferases (HATs) or histone deacetylases (HDACs). Whereas H3K4me3 increases acetylation at promoters via multiple HATs, H3K4me2 targets Set3 HDAC to deacetylate histones in 5' transcribed regions. In 3' regions of genes, H3K36me2/3 facilitates deacetylation by Rpd3S HDAC and slows elongation. Despite their important functions in deacetylation, no strong effects on global gene expression have been seen under optimized or laboratory growth conditions. Instead, H3K4me2-Set3 HDAC and Set2-Rpd3S pathways primarily delay the kinetics of messenger RNA (mRNA) and long noncoding RNA (lncRNA) induction upon environmental changes. A majority of mRNA genes regulated by these pathways have an overlapping lncRNA transcription either from an upstream or an antisense promoter. Surprisingly, the distance between mRNA and lncRNA promoters seems to specify the repressive effects of the two pathways. Given that co-transcriptional methylations and acetylation have been linked to many cancers, studying their functions in a dynamic condition or during cancer progression will be much more important and help identify novel genes associated with cancers.
[Mh] Termos MeSH primário: Histonas/metabolismo
Processamento de Proteína Pós-Traducional
Ativação Transcricional
[Mh] Termos MeSH secundário: Acetilação
Animais
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Metilação
RNA Longo não Codificante/genética
RNA Longo não Codificante/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Histones); 0 (RNA, Long Noncoding); 0 (RNA, Messenger)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180224
[Lr] Data última revisão:
180224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1038/emm.2017.19


  8 / 18716 MEDLINE  
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[PMID]:27776347
[Au] Autor:Zhou Y; Song T; Peng J; Zhou Z; Wei H; Zhou R; Jiang S; Peng J
[Ad] Endereço:State Key Laboratory of Agricultural Microbiology, Division of Animal Infectious Disease, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, P. R. China.
[Ti] Título:SIRT1 suppresses adipogenesis by activating Wnt/ß-catenin signaling in vivo and in vitro.
[So] Source:Oncotarget;7(47):77707-77720, 2016 Nov 22.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sirtuin 1 (SIRT1) regulates adipocyte and osteoblast differentiation. However, the underlying mechanism should be investigated. This study revealed that SIRT1 acts as a crucial repressor of adipogenesis. RNA-interference-mediated SIRT1 knockdown or genetic ablation enhances adipogenic potential, whereas SIRT1 overexpression inhibits adipogenesis in mesenchymal stem cells (MSCs). SIRT1 also deacetylates the histones of sFRP1, sFRP2, and Dact1 promoters; inhibits the mRNA expression of sFRP1, sFRP2, and Dact1; activates Wnt signaling pathways; and suppresses adipogenesis. SIRT1 deacetylates ß-catenin to promote its accumulation in the nucleus and thus induces the transcription of genes that block MSC adipogenesis. In mice, the partial absence of SIRT1 promotes the formation of white adipose tissues without affecting the development of the body of mice. Our study described the regulatory role of SIRT1 in Wnt signaling and proposed a regulatory mechanism of adipogenesis.
[Mh] Termos MeSH primário: Adipogenia
Sirtuína 1/genética
Sirtuína 1/metabolismo
Via de Sinalização Wnt
[Mh] Termos MeSH secundário: Acetilação
Animais
Diferenciação Celular
Linhagem Celular
Técnicas de Silenciamento de Genes
Histonas/metabolismo
Técnicas In Vitro
Células Mesenquimais Estromais/citologia
Células Mesenquimais Estromais/metabolismo
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histones); EC 3.5.1.- (Sirt1 protein, mouse); EC 3.5.1.- (Sirtuin 1)
[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:161025
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.12774


  9 / 18716 MEDLINE  
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[PMID]:29293588
[Au] Autor:Lyman M; Rubinfeld B; Leif R; Mulcahy H; Dugan L; Souza B
[Ad] Endereço:Biosciences and Biotechnology Division, Lawrence Livermore National Laboratory, Livermore, California, United States of America.
[Ti] Título:Rhodotorula taiwanensis MD1149 produces hypoacetylated PEFA compounds with increased surface activity compared to Rhodotorula babjevae MD1169.
[So] Source:PLoS One;13(1):e0190373, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Biosurfactants have several desirable characteristics in the industrial sector: detergency, antimicrobial effects, skin hydration, and emulsibility. Several yeast glycolipids are currently being utilized in these capacities: sophorolipids, ustilagic acid, and mannosylerythritol lipids (MELs). An emerging class of glycolipids, termed polyol esters of fatty acids (PEFA), have recently been reported for Rhodotorula babjevae, a basidiomycetous yeast species that secretes hyperacetylated congeners of PEFA (typically with 3-6 acetylation modifications). While screening Rhodotorula species for surfactant production, we identified a new environmental isolate identified as Rhodotorula taiwanensis MD1149 that dropped the surface tension of the liquid medium, indicating that it produced a potent biosurfactant. Acid depolymerization of the purified biosurfactants, followed by gas chromatography-mass spectrometry (GC-MS) analysis revealed that the biosurfactants were composed of PEFA compounds composed mainly of mannitol and arabitol esters of 3-hydroxy fatty acid, 3-methoxy fatty acid, and fatty acids with a single double bond; chain lengths were mainly C16 and C18. Liquid chromatography-mass spectrometry (LC-MS) confirmed the predicted accurate mass of these compounds. Interestingly, PEFA compounds produced by Rhodotorula taiwanensis MD1149 were more surface active due to their hypoacetylation profile (0-4 acetylation modifications) compared to Rhodotorula babjevae MD1169. These disparate surface active properties, based on acetylation, change the hydrophilic-lipophilic balance (HLB) of these compounds, and their potential utility within industrial applications.
[Mh] Termos MeSH primário: Ácidos Graxos/biossíntese
Polímeros/metabolismo
Rhodotorula/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Cromatografia Líquida de Alta Pressão
Ésteres
Ácidos Graxos/metabolismo
Cromatografia Gasosa-Espectrometria de Massas
Interações Hidrofóbicas e Hidrofílicas
Peso Molecular
Rhodotorula/classificação
Extração em Fase Sólida
Especificidade da Espécie
Espectrometria de Massas por Ionização por Electrospray
Tensão Superficial
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Esters); 0 (Fatty Acids); 0 (Polymers); 0 (polyol)
[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:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190373


  10 / 18716 MEDLINE  
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[PMID]:29233643
[Au] Autor:Wood M; Rymarchyk S; Zheng S; Cen Y
[Ad] Endereço:Department of Pharmaceutical Sciences, Albany College of Pharmacy and Health Sciences, 261 Mountain View Drive, Colchester, VT 05446, USA.
[Ti] Título:Trichostatin A inhibits deacetylation of histone H3 and p53 by SIRT6.
[So] Source:Arch Biochem Biophys;638:8-17, 2018 01 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:SIRT6 is an epigenetic modification enzyme that regulates gene transcription through its deacetylase activity. In addition to histone protein, SIRT6 also modify other proteins and enzymes, some of which are central players in metabolic reprogramming and aging process. Therefore, SIRT6 has emerged as a therapeutic target for the treatment of metabolic disorder and age-related diseases. Here, we report that SIRT6 deacetylates lysine 382 of p53 in short synthetic peptide sequence and in full length p53. Further studies showed that the deacetylation of H3K9Ac and p53K382Ac are insensitive to nicotinamide inhibition, but are sensitive to trichostatin A (TSA) inhibition. Detailed kinetic analysis revealed that TSA competes with the peptide substrate for inhibition, and this inhibition is unique to SIRT6 in the sirtuin family. Taken together, this study not only suggests potential roles of SIRT6 in regulating apoptosis and stress resistance via direct deacetylation of p53, but also provides lead compound for the development of potent and selective SIRT6 inhibitors.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Histonas
Ácidos Hidroxâmicos/farmacologia
Sirtuínas
Proteína Supressora de Tumor p53
[Mh] Termos MeSH secundário: Acetilação/efeitos dos fármacos
Células HEK293
Histonas/química
Histonas/metabolismo
Seres Humanos
Peptídeos/química
Peptídeos/farmacologia
Sirtuínas/química
Sirtuínas/metabolismo
Proteína Supressora de Tumor p53/química
Proteína Supressora de Tumor p53/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Histones); 0 (Hydroxamic Acids); 0 (Peptides); 0 (TP53 protein, human); 0 (Tumor Suppressor Protein p53); 3X2S926L3Z (trichostatin A); EC 3.5.1.- (SIRT6 protein, human); EC 3.5.1.- (Sirtuins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE



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