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  1 / 2243 MEDLINE  
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[PMID]:29360842
[Au] Autor:Liu F; Yang Y; Gao J; Ma C; Bi Y
[Ad] Endereço:College of Life Science, Shandong Normal University, Jinan, China.
[Ti] Título:A comparative transcriptome analysis of a wild purple potato and its red mutant provides insight into the mechanism of anthocyanin transformation.
[So] Source:PLoS One;13(1):e0191406, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this study, a red mutant was obtained through in vitro regeneration of a wild purple potato. High-performance liquid chromatography and Mass spectrometry analysis revealed that pelargonidin-3-O-glucoside and petunidin-3-O-glucoside were main anthocyanins in the mutant and wild type tubers, respectively. In order to thoroughly understand the mechanism of anthocyanin transformation in two materials, a comparative transcriptome analysis of the mutant and wild type was carried out through high-throughput RNA sequencing, and 295 differentially expressed genes (DEGs) were obtained. Real-time qRT-PCR validation of DEGs was consistent with the transcriptome date. The DEGs mainly influenced biological and metabolic pathways, including phenylpropanoid biosynthesis and translation, and biosynthesis of flavone and flavonol. In anthocyanin biosynthetic pathway, the analysis of structural genes expressions showed that three genes, one encoding phenylalanine ammonia-lyase, one encoding 4-coumarate-CoA ligase and one encoding flavonoid 3',5'-hydroxylasem were significantly down-regulated in the mutant; one gene encoding phenylalanine ammonia-lyase was significantly up-regulated. Moreover, the transcription factors, such as bZIP family, MYB family, LOB family, MADS family, zf-HD family and C2H2 family, were significantly regulated in anthocyanin transformation. Response proteins of hormone, such as gibberellin, abscisic acid and brassinosteroid, were also significantly regulated in anthocyanin transformation. The information contributes to discovering the candidate genes in anthocyanin transformation, which can serve as a comprehensive resource for molecular mechanism research of anthocyanin transformation in potatoes.
[Mh] Termos MeSH primário: Antocianinas/biossíntese
Antocianinas/genética
Solanum tuberosum/genética
Solanum tuberosum/metabolismo
[Mh] Termos MeSH secundário: Vias Biossintéticas/genética
Coenzima A Ligases/genética
Sistema Enzimático do Citocromo P-450/genética
Perfilação da Expressão Gênica
Regulação da Expressão Gênica de Plantas
Genes de Plantas
Glucosídeos/biossíntese
Glucosídeos/genética
Sequenciamento de Nucleotídeos em Larga Escala
Mutação
Fenilalanina Amônia-Liase/genética
Pigmentação/genética
Reguladores de Crescimento de Planta/genética
Proteínas de Plantas/genética
Tubérculos/genética
Tubérculos/metabolismo
RNA de Plantas/genética
Fatores de Transcrição/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anthocyanins); 0 (Glucosides); 0 (Plant Growth Regulators); 0 (Plant Proteins); 0 (RNA, Plant); 0 (Transcription Factors); 6988-81-4 (petunidin-3-glucoside); 8H1WZY9R6P (pelargonidin-3-glucoside); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 1.14.- (flavonoid 3',5'-hydroxylase); EC 4.3.1.24 (Phenylalanine Ammonia-Lyase); EC 6.2.1.- (Coenzyme A Ligases); EC 6.2.1.12 (4-coumarate-CoA ligase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180124
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191406


  2 / 2243 MEDLINE  
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[PMID]:28455448
[Au] Autor:Goodrich AC; Meyers DJ; Frueh DP
[Ad] Endereço:From the Department of Biophysics and Biophysical Chemistry and.
[Ti] Título:Molecular impact of covalent modifications on nonribosomal peptide synthetase carrier protein communication.
[So] Source:J Biol Chem;292(24):10002-10013, 2017 06 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nonribosomal peptide synthesis involves the interplay between covalent protein modifications, conformational fluctuations, catalysis, and transient protein-protein interactions. Delineating the mechanisms involved in orchestrating these various processes will deepen our understanding of domain-domain communication in nonribosomal peptide synthetases (NRPSs) and lay the groundwork for the rational reengineering of NRPSs by swapping domains handling different substrates to generate novel natural products. Although many structural and biochemical studies of NRPSs exist, few studies have focused on the energetics and dynamics governing the interactions in these systems. Here, we present detailed binding studies of an adenylation domain and its partner carrier protein in apo-, holo-, and substrate-loaded forms. Results from fluorescence anisotropy, isothermal titration calorimetry, and NMR titrations indicated that covalent modifications to a carrier protein modulate domain communication, suggesting that chemical modifications to carrier proteins during NRPS synthesis may impart directionality to sequential NRPS domain interactions. Comparison of the structure and dynamics of an apo-aryl carrier protein with those of its modified forms revealed structural fluctuations induced by post-translational modifications and mediated by modulations of protein dynamics. The results provide a comprehensive molecular description of a carrier protein throughout its life cycle and demonstrate how a network of dynamic residues can propagate the molecular impact of chemical modifications throughout a protein and influence its affinity toward partner domains.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Proteínas de Transporte/metabolismo
Coenzima A Ligases/metabolismo
Modelos Moleculares
Peptídeo Sintases/metabolismo
Modificação Traducional de Proteínas
Processamento de Proteína Pós-Traducional
Yersinia pestis/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Apoenzimas/química
Apoenzimas/genética
Apoenzimas/metabolismo
Apoproteínas/química
Apoproteínas/genética
Apoproteínas/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Calorimetria
Isótopos de Carbono
Proteínas de Transporte/química
Proteínas de Transporte/genética
Coenzima A Ligases/química
Coenzima A Ligases/genética
Polarização de Fluorescência
Holoenzimas/química
Holoenzimas/genética
Holoenzimas/metabolismo
Cinética
Mutação
Isótopos de Nitrogênio
Ressonância Magnética Nuclear Biomolecular
Peptídeo Sintases/química
Peptídeo Sintases/genética
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Titulometria
Yersinia pestis/enzimologia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Apoenzymes); 0 (Apoproteins); 0 (Bacterial Proteins); 0 (Carbon Isotopes); 0 (Carrier Proteins); 0 (Holoenzymes); 0 (Nitrogen Isotopes); 0 (Recombinant Proteins); EC 6.2.1.- (Coenzyme A Ligases); EC 6.2.1.- (YbtE protein, Yersinia pestis); EC 6.3.2.- (Peptide Synthases); EC 6.3.2.- (non-ribosomal peptide synthase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.766220


  3 / 2243 MEDLINE  
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[PMID]:28884816
[Au] Autor:Ferreira R; Gatto F; Nielsen J
[Ad] Endereço:Department of Biology and Biological Engineering, Systems and Synthetic Biology, Chalmers University of Technology, Gothenburg, Sweden.
[Ti] Título:Exploiting off-targeting in guide-RNAs for CRISPR systems for simultaneous editing of multiple genes.
[So] Source:FEBS Lett;591(20):3288-3295, 2017 Oct.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Bioinformatics tools to design guide-RNAs (gRNAs) in Clustered Regularly Interspaced Short Palindromic Repeats systems mostly focused on minimizing off-targeting to enhance efficacy of genome editing. However, there are circumstances in which off-targeting might be desirable to target multiple genes simultaneously with a single gRNA. We termed these gRNAs as promiscuous gRNAs. Here, we present a computational workflow to identify promiscuous gRNAs that putatively bind to the region of interest for a defined list of genes in a genome. We experimentally validated two promiscuous gRNA for gene deletion, one targeting FAA1 and FAA4 and one targeting PLB1 and PLB2, thus demonstrating that multiplexed genome editing through design of promiscuous gRNA can be performed in a time and cost-effective manner.
[Mh] Termos MeSH primário: Sistemas CRISPR-Cas
Biologia Computacional/métodos
Edição de Genes/métodos
Genoma Fúngico
RNA Guia/genética
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Acil Coenzima A/genética
Acil Coenzima A/metabolismo
Sequência de Bases
Repetições Palindrômicas Curtas Agrupadas e Regularmente Espaçadas
Coenzima A Ligases/genética
Coenzima A Ligases/metabolismo
Deleção de Genes
Expressão Gênica
Lisofosfolipase/genética
Lisofosfolipase/metabolismo
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
RNA Guia/metabolismo
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Membrane Proteins); 0 (RNA, Guide); 0 (Saccharomyces cerevisiae Proteins); EC 3.1.1.5 (Lysophospholipase); EC 3.1.1.5 (PLB1 protein, S cerevisiae); EC 3.1.1.5 (PLB2 protein, S cerevisiae); EC 6.2.1.- (Coenzyme A Ligases); EC 6.2.1.- (Faa1 protein, S cerevisiae); EC 6.2.1.3 (FAA4 protein, S cerevisiae)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12835


  4 / 2243 MEDLINE  
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[PMID]:28771887
[Au] Autor:Migita T; Takayama KI; Urano T; Obinata D; Ikeda K; Soga T; Takahashi S; Inoue S
[Ad] Endereço:Departments of Anti-Aging Medicine and Geriatric Medicine, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
[Ti] Título:ACSL3 promotes intratumoral steroidogenesis in prostate cancer cells.
[So] Source:Cancer Sci;108(10):2011-2021, 2017 Oct.
[Is] ISSN:1349-7006
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Long-chain acyl-coenzyme A (CoA) synthetase 3 (ACSL3) is an androgen-responsive gene involved in the generation of fatty acyl-CoA esters. ACSL3 is expressed in both androgen-sensitive and castration-resistant prostate cancer (CRPC). However, its role in prostate cancer remains elusive. We overexpressed ACSL3 in androgen-dependent LNCaP cells and examined the downstream effectors of ACSL3. Furthermore, we examined the role of ACSL3 in the androgen metabolism of prostate cancer. ACSL3 overexpression led to upregulation of several genes such as aldo-keto reductase 1C3 (AKR1C3) involved in steroidogenesis, which utilizes adrenal androgen dehydroepiandrosterone sulfate (DHEAS) as substrate, and downregulated androgen-inactivating enzyme UDP-glucuronosyltransferase 2 (UGT2B). Exposure to DHEAS significantly increased testosterone levels and cell proliferative response in ACSL3-overexpressing cells when compared to that in control cells. A public database showed that ACSL3 level was higher in CRPC than in hormone-sensitive prostate cancer. CRPC cells showed an increased expression of ACSL3 and an expression pattern of AKR1C3 and UGT2B similar to ACSL3-overexpressing cells. DHEAS stimulation significantly promoted the proliferation of CRPC cells when compared to that of LNCaP cells. These findings suggest that ACSL3 contributes to the growth of CRPC through intratumoral steroidogenesis (i.e. promoting androgen synthesis from DHEAS and preventing the catabolism of active androgens).
[Mh] Termos MeSH primário: Coenzima A Ligases/genética
Coenzima A Ligases/metabolismo
Sulfato de Desidroepiandrosterona/farmacologia
Neoplasias de Próstata Resistentes à Castração/metabolismo
Testosterona/metabolismo
[Mh] Termos MeSH secundário: 3-Hidroxiesteroide Desidrogenases/metabolismo
Membro C3 da Família 1 de alfa-Ceto Redutase
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Glucuronosiltransferase/metabolismo
Seres Humanos
Hidroxiprostaglandina Desidrogenases/metabolismo
Lipogênese
Masculino
Neoplasias de Próstata Resistentes à Castração/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
3XMK78S47O (Testosterone); 57B09Q7FJR (Dehydroepiandrosterone Sulfate); EC 1.1.- (3-Hydroxysteroid Dehydrogenases); EC 1.1.1.- (Hydroxyprostaglandin Dehydrogenases); EC 1.1.1.357 (AKR1C3 protein, human); EC 1.1.1.357 (Aldo-Keto Reductase Family 1 Member C3); EC 2.4.1.17 (Glucuronosyltransferase); EC 6.2.1.- (Coenzyme A Ligases); EC 6.2.1.3 (long-chain-fatty-acid-CoA ligase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE
[do] DOI:10.1111/cas.13339


  5 / 2243 MEDLINE  
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[PMID]:28655762
[Au] Autor:Yadav PK; Rajasekharan R
[Ad] Endereço:From the Lipidomic Centre, Department of Lipid Science, and.
[Ti] Título:The m A methyltransferase Ime4 epitranscriptionally regulates triacylglycerol metabolism and vacuolar morphology in haploid yeast cells.
[So] Source:J Biol Chem;292(33):13727-13744, 2017 Aug 18.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:-Methyladenosine (m A) is among the most common modifications in eukaryotic mRNA. The role of yeast m A methyltransferase, Ime4, in meiosis and sporulation in diploid strains is very well studied, but its role in haploid strains has remained unknown. Here, with the help of an immunoblotting strategy and Ime4-GFP protein localization studies, we establish the physiological role of Ime4 in haploid cells. Our data showed that Ime4 epitranscriptionally regulates triacylglycerol metabolism and vacuolar morphology through the long-chain fatty acyl-CoA synthetase Faa1, independently of the RNA methylation complex (MIS complex). The MIS complex consists of the Ime4, Mum2, and Slz1 proteins. Our affinity enrichment strategy (methylated RNA immunoprecipitation assays) using m A polyclonal antibodies coupled with mRNA isolation, quantitative real-time PCR, and standard PCR analyses confirmed the presence of m A-modified transcripts in haploid yeast cells. The term "epitranscriptional regulation" encompasses the RNA modification-mediated regulation of genes. Moreover, we demonstrate that the Aft2 transcription factor up-regulates expression. Because the m A methylation machinery is fundamentally conserved throughout eukaryotes, our findings will help advance the rapidly emerging field of RNA epitranscriptomics. The metabolic link identified here between m A methylation and triacylglycerol metabolism via the Ime4 protein provides new insights into lipid metabolism and the pathophysiology of lipid-related metabolic disorders, such as obesity. Because the yeast vacuole is an analogue of the mammalian lysosome, our findings pave the way to better understand the role of m A methylation in lysosome-related functions and diseases.
[Mh] Termos MeSH primário: Fator 2 Ativador da Transcrição/metabolismo
Coenzima A Ligases/metabolismo
Metiltransferases/metabolismo
Processamento Pós-Transcricional do RNA
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/fisiologia
Vacúolos/metabolismo
[Mh] Termos MeSH secundário: Fator 2 Ativador da Transcrição/genética
Substituição de Aminoácidos
Proteínas de Ciclo Celular/química
Proteínas de Ciclo Celular/genética
Proteínas de Ciclo Celular/metabolismo
Coenzima A Ligases/genética
Diploide
Epigênese Genética
Deleção de Genes
Regulação Fúngica da Expressão Gênica
Haploidia
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Metilação
Metiltransferases/química
Metiltransferases/genética
Microscopia Eletrônica de Varredura
Mutagênese Sítio-Dirigida
Mutação
Tamanho das Organelas
Proteínas Recombinantes de Fusão/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/ultraestrutura
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Triglicerídeos/metabolismo
Vacúolos/ultraestrutura
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Activating Transcription Factor 2); 0 (Cell Cycle Proteins); 0 (Luminescent Proteins); 0 (Mum2 protein, S cerevisiae); 0 (Recombinant Fusion Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (Slz1 protein, S cerevisiae); 0 (Triglycerides); EC 2.1.1.- (Methyltransferases); EC 2.1.1.- (mRNA(adenine-N6)-methyltransferase); EC 6.2.1.- (Coenzyme A Ligases); EC 6.2.1.- (Faa1 protein, S cerevisiae)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170629
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.783761


  6 / 2243 MEDLINE  
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[PMID]:28644952
[Au] Autor:Lombard DB; Zhao Y
[Ad] Endereço:Department of Pathology and Institute of Gerontology, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: davidlom@med.umich.edu.
[Ti] Título:ACSF3 and Mal(onate)-Adapted Mitochondria.
[So] Source:Cell Chem Biol;24(6):649-650, 2017 Jun 22.
[Is] ISSN:2451-9456
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this issue of Cell Chemical Biology, Bowman and colleagues show that the mitochondrial enzyme ACSF3 generates malonyl-CoA from malonate, in turn regulating metabolic flux and mitochondrial protein malonylation (Bowman et al., 2017). The study reveals a mechanism to generate mitochondrial malonyl-CoA and how this molecule impacts mitochondrial biology.
[Mh] Termos MeSH primário: Coenzima A Ligases/metabolismo
Malonatos/metabolismo
Mitocôndrias/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Malonil Coenzima A/metabolismo
Camundongos
Proteínas Mitocondriais/metabolismo
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Malonates); 0 (Mitochondrial Proteins); 524-14-1 (Malonyl Coenzyme A); 9KX7ZMG0MK (malonic acid); EC 6.2.1.- (ACSF3 protein, human); EC 6.2.1.- (Coenzyme A Ligases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE


  7 / 2243 MEDLINE  
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[PMID]:28636641
[Au] Autor:Vancraenenbroeck R; Kunzelmann S; Webb MR
[Ad] Endereço:The Francis Crick Institute, London, United Kingdom.
[Ti] Título:Development of a range of fluorescent reagentless biosensors for ATP, based on malonyl-coenzyme A synthetase.
[So] Source:PLoS One;12(6):e0179547, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The range of ATP concentrations that can be measured with a fluorescent reagentless biosensor for ATP has been increased by modulating its affinity for this analyte. The ATP biosensor is an adduct of two tetramethylrhodamines with MatB from Rhodopseudomonas palustris. Mutations were introduced into the binding site to modify ATP binding affinity, while aiming to maintain the concomitant fluorescence signal. Using this signal, the effect of mutations in different parts of the binding site was measured. This mutational analysis revealed three variants in particular, each with a single mutation in the phosphate-binding loop, which had potentially beneficial changes in ATP binding properties but preserving a fluorescence change of ~3-fold on ATP binding. Two variants (T167A and T303A) weakened the binding, changing the dissociation constant from the parent's 6 µM to 123 µM and 42 µM, respectively. Kinetic measurements showed that the effect of these mutations on affinity was by an increase in dissociation rate constants. These variants widen the range of ATP concentration that can be measured readily by this biosensor to >100 µM. In contrast, a third variant, S170A, decreased the dissociation constant of ATP to 3.8 µM and has a fluorescence change of 4.2 on binding ATP. This variant has increased selectivity for ATP over ADP of >200-fold. This had advantages over the parent by increasing sensitivity as well as increasing selectivity during ATP measurements in which ADP is present.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/análise
Proteínas de Bactérias/metabolismo
Técnicas Biossensoriais
Coenzima A Ligases/metabolismo
Corantes Fluorescentes/química
[Mh] Termos MeSH secundário: Difosfato de Adenosina/química
Difosfato de Adenosina/metabolismo
Trifosfato de Adenosina/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Sítios de Ligação
Coenzima A Ligases/química
Coenzima A Ligases/genética
Cinética
Simulação de Dinâmica Molecular
Mutagênese Sítio-Dirigida
Ligação Proteica
Estrutura Terciária de Proteína
Piruvato Quinase/química
Piruvato Quinase/metabolismo
Rodaminas/química
Rodopseudomonas/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Fluorescent Dyes); 0 (Rhodamines); 61D2G4IYVH (Adenosine Diphosphate); 62669-72-1 (tetramethylrhodamine); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.1.40 (Pyruvate Kinase); EC 6.2.1.- (Coenzyme A Ligases); EC 6.2.1.- (malonyl-CoA synthetase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179547


  8 / 2243 MEDLINE  
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[PMID]:28522731
[Au] Autor:Zabielski P; Chacinska M; Charkiewicz K; Baranowski M; Gorski J; Blachnio-Zabielska AU
[Ad] Endereço:Department of Medical BiologyMedical University of Bialystok, Bialystok, Poland.
[Ti] Título:Effect of metformin on bioactive lipid metabolism in insulin-resistant muscle.
[So] Source:J Endocrinol;233(3):329-340, 2017 Jun.
[Is] ISSN:1479-6805
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Intramuscular accumulation of bioactive lipids leads to insulin resistance and type 2 diabetes (T2D). There is lack of consensus concerning which of the lipid mediators has the greatest impact on muscle insulin action Our aim was to elucidate the effects of high-fat diet (HFD) and metformin (Met) on skeletal muscle bioactive lipid accumulation and insulin resistance (IR) in rats. We employed a [U- C]palmitate isotope tracer and mass spectrometry to measure the content and fractional synthesis rate (FSR) of intramuscular long-chain acyl-CoA (LCACoA), diacylglycerols (DAG) and ceramide (Cer). Eight weeks of HFD-induced intramuscular accumulation of LCACoA, DAG and Cer accompanied by both systemic and skeletal muscle IR. Metformin treatment improved insulin sensitivity at both systemic and muscular level by the augmentation of Akt/PKB and AS160 phosphorylation and decreased the content of DAG and Cer and their respective FSR. Principal component analysis (PCA) of lipid variables revealed that altered skeletal muscle IR was associated with lipid species containing 18-carbon acyl-chain, especially with C18:0-Cer, C18:1-Cer, 18:0/18:2-DAG and 18:2/18:2-DAG, but not palmitate-derived lipids. It is concluded that the insulin-sensitizing action of metformin in skeletal muscle is associated with decreased 18-carbon acyl-chain-derived bioactive lipids.
[Mh] Termos MeSH primário: Resistência à Insulina/fisiologia
Metabolismo dos Lipídeos/efeitos dos fármacos
Metformina/farmacologia
Músculo Esquelético/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Coenzima A Ligases/genética
Coenzima A Ligases/metabolismo
Dieta Hiperlipídica/efeitos adversos
Proteínas de Transporte de Ácido Graxo/genética
Proteínas de Transporte de Ácido Graxo/metabolismo
Ácidos Graxos não Esterificados/sangue
Regulação da Expressão Gênica/efeitos dos fármacos
Regulação da Expressão Gênica/fisiologia
Masculino
Metformina/administração & dosagem
Músculo Esquelético/metabolismo
Ratos
Ratos Wistar
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acid Transport Proteins); 0 (Fatty Acids, Nonesterified); 9100L32L2N (Metformin); EC 6.2.1.- (Coenzyme A Ligases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170520
[St] Status:MEDLINE
[do] DOI:10.1530/JOE-16-0381


  9 / 2243 MEDLINE  
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[PMID]:28479296
[Au] Autor:Bowman CE; Rodriguez S; Selen Alpergin ES; Acoba MG; Zhao L; Hartung T; Claypool SM; Watkins PA; Wolfgang MJ
[Ad] Endereço:Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA; Center for Metabolism and Obesity Research, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
[Ti] Título:The Mammalian Malonyl-CoA Synthetase ACSF3 Is Required for Mitochondrial Protein Malonylation and Metabolic Efficiency.
[So] Source:Cell Chem Biol;24(6):673-684.e4, 2017 Jun 22.
[Is] ISSN:2451-9456
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Malonyl-coenzyme A (malonyl-CoA) is a central metabolite in mammalian fatty acid biochemistry generated and utilized in the cytoplasm; however, little is known about noncanonical organelle-specific malonyl-CoA metabolism. Intramitochondrial malonyl-CoA is generated by a malonyl-CoA synthetase, ACSF3, which produces malonyl-CoA from malonate, an endogenous competitive inhibitor of succinate dehydrogenase. To determine the metabolic requirement for mitochondrial malonyl-CoA, ACSF3 knockout (KO) cells were generated by CRISPR/Cas-mediated genome editing. ACSF3 KO cells exhibited elevated malonate and impaired mitochondrial metabolism. Unbiased and targeted metabolomics analysis of KO and control cells in the presence or absence of exogenous malonate revealed metabolic changes dependent on either malonate or malonyl-CoA. While ACSF3 was required for the metabolism and therefore detoxification of malonate, ACSF3-derived malonyl-CoA was specifically required for lysine malonylation of mitochondrial proteins. Together, these data describe an essential role for ACSF3 in dictating the metabolic fate of mitochondrial malonate and malonyl-CoA in mammalian metabolism.
[Mh] Termos MeSH primário: Coenzima A Ligases/metabolismo
Malonatos/metabolismo
Mitocôndrias/metabolismo
Proteínas Mitocondriais/metabolismo
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Acilação
Animais
Linhagem Celular
Coenzima A Ligases/deficiência
Coenzima A Ligases/genética
Técnicas de Inativação de Genes
Seres Humanos
Lipogênese
Camundongos
Mutação
Especificidade de Órgãos
Oxirredução
Engenharia de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Malonates); 0 (Mitochondrial Proteins); 9KX7ZMG0MK (malonic acid); EC 6.2.1.- (ACSF3 protein, human); EC 6.2.1.- (Coenzyme A Ligases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170719
[Lr] Data última revisão:
170719
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170509
[St] Status:MEDLINE


  10 / 2243 MEDLINE  
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[PMID]:28414711
[Au] Autor:Estrada P; Manandhar M; Dong SH; Deveryshetty J; Agarwal V; Cronan JE; Nair SK
[Ad] Endereço:Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
[Ti] Título:The pimeloyl-CoA synthetase BioW defines a new fold for adenylate-forming enzymes.
[So] Source:Nat Chem Biol;13(6):668-674, 2017 Jun.
[Is] ISSN:1552-4469
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Reactions that activate carboxylates through acyl-adenylate intermediates are found throughout biology and include acyl- and aryl-CoA synthetases and tRNA synthetases. Here we describe the characterization of Aquifex aeolicus BioW, which represents a new protein fold within the superfamily of adenylating enzymes. Substrate-bound structures identified the enzyme active site and elucidated the mechanistic strategy for conjugating CoA to the seven-carbon α,ω-dicarboxylate pimelate, a biotin precursor. Proper position of reactive groups for the two half-reactions is achieved solely through movements of active site residues, as confirmed by site-directed mutational analysis. The ability of BioW to hydrolyze adenylates of noncognate substrates is reminiscent of pre-transfer proofreading observed in some tRNA synthetases, and we show that this activity can be abolished by mutation of a single residue. These studies illustrate how BioW can carry out three different biologically prevalent chemical reactions (adenylation, thioesterification, and proofreading) in the context of a new protein fold.
[Mh] Termos MeSH primário: Monofosfato de Adenosina/metabolismo
Coenzima A Ligases/química
Modelos Moleculares
[Mh] Termos MeSH secundário: Monofosfato de Adenosina/química
Domínio Catalítico
Coenzima A Ligases/metabolismo
Cristalização
Ligantes
Estrutura Molecular
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ligands); 415SHH325A (Adenosine Monophosphate); EC 6.2.1.- (Coenzyme A Ligases); EC 6.2.1.- (pimeloyl-CoA synthetase)
[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:170418
[St] Status:MEDLINE
[do] DOI:10.1038/nchembio.2359



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