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Pesquisa : D08.811.913.050.134 [Categoria DeCS]
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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


  2 / 8416 MEDLINE  
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[PMID]:29287723
[Au] Autor:Yan J; Liang X; Cui Y; Cao X; Gao J
[Ad] Endereço:College of Fisheries, Key Lab of Agricultural Animal Genetics, Breeding and Reproduction of Ministry of Education/Key Lab of Freshwater Animal Breeding, Ministry of Agriculture, Huazhong Agricultural University, Wuhan 430070, China.
[Ti] Título:Elovl4 can effectively elongate C18 polyunsaturated fatty acids in loach Misgurnus anguillicaudatus.
[So] Source:Biochem Biophys Res Commun;495(4):2637-2642, 2018 01 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this study, full-length cDNA sequences of elovl4a and elovl4b from loach Misgurnus anguillicaudatus were cloned. The full-length cDNAs of loach elovl4a and elovl4b were 2423 and 2054bp, encoding 315 and 300 amino acids, respectively. The deduced amino acid sequences of elovl4a and elovl4b in loach both shared the highest identity with those of Danio rerio, whereas lower identity score between loach elovl4a and elovl4b was present. Temporal expression and tissue expression of loach elovl4a and elovl4b were studied by reverse transcriptase PCR. Results of the tissue expression analyses suggested different functions of loach elovl4a and elovl4b. Functional characterizations of loach elovl4a and elovl4b on synthesis of fatty acids, especially elongating C18 polyunsaturated fatty acids (PUFAs) to longer-chain fatty acids, were studied by heterologous expression in Saccharomyces cerevisiae. Loach elovl4a and elvol4b enzymes were able to elongate all fatty acids tested including 18:2n-6, 18:3n-3, 18:3n-6, 20:4n-6 and 20:5n-3. At last, expression levels of the two elovl4 genes of loach fin cells incubated with 18:2n-6 and 18:3n-3 of different concentrations were measured. Expressions of elovl4a and elovl4b of loach fin cells were significantly up-regulated by 18:2n-6 and 18:3n-3. The results obtained here indicated that loach elovl4 could effectively elongate C18 PUFAs. This was a systematic report of elovl4's elongating functions towards C18 and provided an alternative pathway for C20 biosynthesis in fish species.
[Mh] Termos MeSH primário: Acetiltransferases/química
Acetiltransferases/metabolismo
Cipriniformes/metabolismo
Ácidos Graxos Insaturados/química
Ácidos Graxos Insaturados/metabolismo
Metabolismo dos Lipídeos/fisiologia
[Mh] Termos MeSH secundário: Animais
Peso Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fatty Acids, Unsaturated); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (fatty acid elongases)
[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:171231
[St] Status:MEDLINE


  3 / 8416 MEDLINE  
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[PMID]:29307827
[Au] Autor:Manning ME; Danson EJ; Calderone CT
[Ad] Endereço:Department of Chemistry, Carleton College, 1 North College Street, Northfield, MN 55057, United States.
[Ti] Título:Functional chararacterization of the enzymes TabB and TabD involved in tabtoxin biosynthesis by Pseudomonas syringae.
[So] Source:Biochem Biophys Res Commun;496(1):212-217, 2018 01 29.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pseudomonas syringae pv. tabaci ATCC 11528 produces tabtoxin, a ß-lactam-containing dipeptide phytotoxin. Tabtoxinine-ß-lactam (TßL), one of tabtoxin's constituent amino acids, structurally mimics lysine, and many of the proteins encoded by the tabtoxin biosynthetic gene cluster are homologs of lysine biosynthetic enzymes, suggesting that the tabtoxin and lysine biosynthetic routes parallel one another. We cloned and expressed TabB and TabD, predicted homologs of tetrahydrodipicolinate (THDPA)-N-acyltransferase and N-acyl-THDPA aminotransferase, respectively, to determine their activities in vitro. We confirmed that TabB succinylates THDPA and that TabD is a PLP-dependent aminotransferase that utilizes glutamate as an amine donor. Surprisingly, we also found that though TabD could utilize the TabB product N-succinyl-THDPA as a substrate, THDPA itself was also recognized. These observations reveal that TabB functionally duplicates DapD, the THDPA-N-succinyltransferase involved in lysine biosynthesis, and reinforce the close relationship between the metabolic logics underpinning the respective biosynthetic pathways.
[Mh] Termos MeSH primário: Acetiltransferases/química
Acetiltransferases/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Dipeptídeos/biossíntese
Pseudomonas syringae/metabolismo
Transaminases/química
Transaminases/metabolismo
[Mh] Termos MeSH secundário: Ativação Enzimática
Estabilidade Enzimática
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Dipeptides); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (TabB protein, Pseudomonas syringae); EC 2.6.1.- (Transaminases); H3YX70R64N (tabtoxin)
[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:180109
[St] Status:MEDLINE


  4 / 8416 MEDLINE  
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[PMID]:29330052
[Au] Autor:Chen H; Zhang L; He W; Liu T; Zhao Y; Chen H; Li Y
[Ad] Endereço:Institute of Cell Biology, School of Life Sciences, Lanzhou University, 222 Tian-Shui South Road, Lanzhou 730000, Gansu, China; Institute of Medical Physiology and Psychology, School of Basic Medical Sciences, Lanzhou University, 199 Dong-Gang West Road, Lanzhou 730000, Gansu, China. Electronic addr
[Ti] Título:ESCO2 knockdown inhibits cell proliferation and induces apoptosis in human gastric cancer cells.
[So] Source:Biochem Biophys Res Commun;496(2):475-481, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Establishment of cohesion 1 homolog 2 (ESCO2), an essential gene for cohesion regulation and genomic stability, has not been studied in human gastric cancer (GC). We found that ESCO2 knockdown in human GC cell lines dramatically inhibited cell proliferation and induced cell apoptosis in vitro and suppressed tumor xenograft development in vivo. Furthermore, adenosine monophosphate-activated protein kinase (AMPK) was activated following the suppression of its downstream targets, including mammalian target of rapamycin (mTOR) and p70 ribosomal S6 kinase 1 (p70S6K1), and this result was consistent with p53 activation. Significantly, co-immunoprecipitation (Co-IP) analyses indicated that ESCO2 can interact with p53 in GC cells. Taken together, our data demonstrate that ESCO2 is essential for the development of GC and might be a potential therapeutic target for treating GC.
[Mh] Termos MeSH primário: Acetiltransferases/genética
Proteínas Cromossômicas não Histona/genética
Células Epiteliais/metabolismo
Regulação Neoplásica da Expressão Gênica
Neoplasias Gástricas/genética
Proteína Supressora de Tumor p53/genética
[Mh] Termos MeSH secundário: Proteínas Quinases Ativadas por AMP/genética
Proteínas Quinases Ativadas por AMP/metabolismo
Acetiltransferases/antagonistas & inibidores
Acetiltransferases/metabolismo
Animais
Apoptose/genética
Linhagem Celular Tumoral
Proliferação Celular
Proteínas Cromossômicas não Histona/antagonistas & inibidores
Proteínas Cromossômicas não Histona/metabolismo
Células Epiteliais/patologia
Feminino
Seres Humanos
Camundongos
Camundongos Endogâmicos BALB C
Camundongos Nus
Ligação Proteica
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Proteínas Quinases S6 Ribossômicas 70-kDa/genética
Proteínas Quinases S6 Ribossômicas 70-kDa/metabolismo
Transdução de Sinais
Neoplasias Gástricas/metabolismo
Neoplasias Gástricas/patologia
Serina-Treonina Quinases TOR/genética
Serina-Treonina Quinases TOR/metabolismo
Proteína Supressora de Tumor p53/metabolismo
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromosomal Proteins, Non-Histone); 0 (RNA, Small Interfering); 0 (Tumor Suppressor Protein p53); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (ESCO2 protein, human); EC 2.7.1.1 (MTOR protein, human); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (PRKAA1 protein, human); EC 2.7.11.1 (Ribosomal Protein S6 Kinases, 70-kDa); EC 2.7.11.1 (ribosomal protein S6 kinase, 70kD, polypeptide 2); EC 2.7.11.31 (AMP-Activated Protein Kinases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180114
[St] Status:MEDLINE


  5 / 8416 MEDLINE  
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[PMID]:29196537
[Au] Autor:Kawasumi R; Abe T; Arakawa H; Garre M; Hirota K; Branzei D
[Ad] Endereço:The FIRC (Italian Foundation for Cancer Research) Institute of Molecular Oncology (IFOM), 20139 Milan, Italy.
[Ti] Título:ESCO1/2's roles in chromosome structure and interphase chromatin organization.
[So] Source:Genes Dev;31(21):2136-2150, 2017 11 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:ESCO1/2 acetyltransferases mediating SMC3 acetylation and sister chromatid cohesion (SCC) are differentially required for genome integrity and development. Here we established chicken DT40 cell lines with mutations in ESCO1/2, SMC3 acetylation, and the cohesin remover WAPL. Both ESCO1 and ESCO2 promoted SCC, while ESCO2 was additionally and specifically required for proliferation and centromere integrity. overexpression fully suppressed the slow proliferation and centromeric separation phenotypes of cells but only partly suppressed its chromosome arm SCC defects. Concomitant inactivation of ESCO1 and ESCO2 caused lethality owing to compromised mitotic chromosome segregation. Neither nor acetyl-mimicking mutations rescued lethality. Notably, conditional mutants showed very severe proliferation defects associated with catastrophic mitoses and also abnormal interphase chromatin organization patterns. The results indicate that cohesion establishment by vertebrate ESCO1/2 is linked to interphase chromatin architecture formation, a newly identified function of cohesin acetyltransferases that is both fundamentally and medically relevant.
[Mh] Termos MeSH primário: Acetiltransferases/metabolismo
Montagem e Desmontagem da Cromatina/genética
Proteínas Cromossômicas não Histona/metabolismo
Estruturas Cromossômicas/genética
Instabilidade Genômica/genética
[Mh] Termos MeSH secundário: Acetilação
Acetiltransferases/genética
Animais
Linhagem Celular
Proliferação Celular/genética
Centrômero/genética
Galinhas
Proteínas Cromossômicas não Histona/genética
Técnicas de Inativação de Genes
Inativação Gênica
Interfase/genética
Proteínas Nucleares/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromosomal Proteins, Non-Histone); 0 (Nuclear Proteins); EC 2.3.1.- (Acetyltransferases)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180130
[Lr] Data última revisão:
180130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171203
[St] Status:MEDLINE
[do] DOI:10.1101/gad.306084.117


  6 / 8416 MEDLINE  
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[PMID]:28461456
[Au] Autor:Zhao H; Matsuzaka T; Nakano Y; Motomura K; Tang N; Yokoo T; Okajima Y; Han SI; Takeuchi Y; Aita Y; Iwasaki H; Yatoh S; Suzuki H; Sekiya M; Yahagi N; Nakagawa Y; Sone H; Yamada N; Shimano H
[Ad] Endereço:Department of Internal Medicine (Endocrinology and Metabolism), Faculty of Medicine, University of Tsukuba, Tsukuba, Ibaraki, Japan.
[Ti] Título:Elovl6 Deficiency Improves Glycemic Control in Diabetic / Mice by Expanding ß-Cell Mass and Increasing Insulin Secretory Capacity.
[So] Source:Diabetes;66(7):1833-1846, 2017 07.
[Is] ISSN:1939-327X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dysfunctional fatty acid (FA) metabolism plays an important role in the pathogenesis of ß-cell dysfunction and loss of ß-cell mass in type 2 diabetes (T2D). Elovl6 is a microsomal enzyme that is responsible for converting C16 saturated and monounsaturated FAs into C18 species. We previously showed that Elovl6 played a critical role in the development of obesity-induced insulin resistance by modifying FA composition. To further define its role in T2D development, we assessed the effects of deletion in leptin receptor-deficient C57BL/KsJ / mice, a model of T2D. The / ; mice had a markedly increased ß-cell mass with increased proliferation and decreased apoptosis, an adaptive increase in insulin, and improved glycemic control. / islets were characterized by a prominent elevation of oleate (C18:1n-9), cell stress, and inflammation, which was completely suppressed by Elovl6 deletion. As a mechanistic ex vivo experiment, isolated islets from mice exhibited reduced susceptibility to palmitate-induced inflammation, endoplasmic reticulum stress, and ß-cell apoptosis. In contrast, oleate-treated islets resulted in impaired glucose-stimulated insulin secretion with suppressed related genes irrespective of the Elovl6 gene. Taken together, Elovl6 is a fundamental factor linking dysregulated lipid metabolism to ß-cell dysfunction, islet inflammation, and ß-cell apoptosis in T2D, highlighting oleate as the potential culprit of ß-cell lipotoxicity.
[Mh] Termos MeSH primário: Acetiltransferases/deficiência
Acetiltransferases/genética
Diabetes Mellitus Experimental/genética
Diabetes Mellitus Tipo 2/genética
Células Secretoras de Insulina/secreção
Insulina/secreção
[Mh] Termos MeSH secundário: Acetiltransferases/fisiologia
Animais
Apoptose/genética
Glicemia/metabolismo
Diabetes Mellitus Experimental/metabolismo
Diabetes Mellitus Tipo 2/metabolismo
Estresse do Retículo Endoplasmático
Ácidos Graxos não Esterificados/metabolismo
Feminino
Imuno-Histoquímica
Técnicas In Vitro
Inflamação/induzido quimicamente
Inflamação/genética
Células Secretoras de Insulina/efeitos dos fármacos
Células Secretoras de Insulina/patologia
Ilhotas Pancreáticas/efeitos dos fármacos
Ilhotas Pancreáticas/patologia
Ilhotas Pancreáticas/secreção
Metabolismo dos Lipídeos/genética
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Ácido Oleico/farmacologia
Tamanho do Órgão
Palmitatos/efeitos adversos
Reação em Cadeia da Polimerase em Tempo Real
Receptores para Leptina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Blood Glucose); 0 (Fatty Acids, Nonesterified); 0 (Insulin); 0 (Palmitates); 0 (Receptors, Leptin); 0 (leptin receptor, mouse); 2UMI9U37CP (Oleic Acid); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (fatty acid elongases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.2337/db16-1277


  7 / 8416 MEDLINE  
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[PMID]:29232376
[Au] Autor:Caliskan G; Baris IC; Ayaydin F; Dobson MJ; Senarisoy M; Boros IM; Topcu Z; Zencir S
[Ad] Endereço:Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Ege University, Izmir, Turkey.
[Ti] Título:Che1/AATF interacts with subunits of the histone acetyltransferase core module of SAGA complexes.
[So] Source:PLoS One;12(12):e0189193, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:General Control Non-derepressible 5 (GCN5) and Alteration/Deficiency in Activation 2 and 3 proteins (ADA2 and ADA3, respectively) are subunits of the Histone AcetylTransferase (HAT) module of SAGA- and ATAC-type co-activators. We previously reported four new interacting partners of human ADA3 identified by screening a human fetal brain cDNA library using yeast two hybrid technology. One of these partners was Apoptosis-Antagonizing Transcription Factor (AATF), also known as Che-1, an RNA polymerase II-binding protein with a number of roles in different cellular processes including regulation of transcription, cell proliferation, cell cycle control, DNA damage responses and apoptosis. Che-1/AATF is a potential therapeutic target for cancer treatments. In this study, we aimed to identify whether besides ADA3, other components of the HAT modules of SAGA and ATAC complexes, human ADA2 and GCN5 also interact with Che-1/AATF. Co-immunoprecipitation and co-localization experiments were used to demonstrate association of AATF both with two ADA2 isoforms, ADA2A and ADA2B and with GCN5 proteins in human cells and yeast two-hybrid assays to delineate domains in the ADA2 and GCN5 proteins required for these interactions. These findings provide new insights into the pathways regulated by ADA-containing protein complexes.
[Mh] Termos MeSH primário: Histona Acetiltransferases/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
Transativadores/metabolismo
[Mh] Termos MeSH secundário: Acetiltransferases/metabolismo
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Seres Humanos
Ligação Proteica
Fatores de Transcrição/metabolismo
Ativação Transcricional
Fatores de Transcrição de p300-CBP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (SAGA complex, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (TADA2A protein, human); 0 (TADA2B protein, human); 0 (Trans-Activators); 0 (Transcription Factors); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (Sgf29 protein, human); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (p300-CBP Transcription Factors); EC 2.3.1.48 (p300-CBP-associated factor)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189193


  8 / 8416 MEDLINE  
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[PMID]:29016658
[Au] Autor:Magin RS; Deng S; Zhang H; Cooperman B; Marmorstein R
[Ad] Endereço:Department of Biochemistry and Biophysics, Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America.
[Ti] Título:Probing the interaction between NatA and the ribosome for co-translational protein acetylation.
[So] Source:PLoS One;12(10):e0186278, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:N-terminal acetylation is among the most abundant protein modifications in eukaryotic cells. Over the last decade, significant progress has been made in elucidating the function of N-terminal acetylation for a number of diverse systems, involved in a wide variety of biological processes. The enzymes responsible for the modification are the N-terminal acetyltransferases (NATs). The NATs are a highly conserved group of enzymes in eukaryotes, which are responsible for acetylating over 80% of the soluble proteome in human cells. Importantly, many of these NATs act co-translationally; they interact with the ribosome near the exit tunnel and acetylate the nascent protein chain as it is being translated. While the structures of many of the NATs have been determined, the molecular basis for the interaction with ribosome is not known. Here, using purified ribosomes and NatA, a very well-studied NAT, we show that NatA forms a stable complex with the ribosome in the absence of other stabilizing factors and through two conserved regions; primarily through an N-terminal domain and an internal basic helix. These regions may orient the active site of the NatA to face the peptide emerging from the exit tunnel. This work provides a framework for understanding how NatA and potentially other NATs interact with the ribosome for co-translational protein acetylation and sets the foundation for future studies to decouple N-terminal acetyltransferase activity from ribosome association.
[Mh] Termos MeSH primário: Acetiltransferases/metabolismo
Biossíntese de Proteínas
Processamento de Proteína Pós-Traducional
Subunidades Proteicas/metabolismo
Ribossomos/metabolismo
Proteínas de Schizosaccharomyces pombe/metabolismo
Schizosaccharomyces/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Acetiltransferases/química
Acetiltransferases/genética
Motivos de Aminoácidos
Sítios de Ligação
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Cinética
Modelos Moleculares
Ligação Proteica
Conformação Proteica em alfa-Hélice
Domínios e Motivos de Interação entre Proteínas
Subunidades Proteicas/química
Subunidades Proteicas/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Ribossomos/química
Ribossomos/genética
Schizosaccharomyces/genética
Proteínas de Schizosaccharomyces pombe/química
Proteínas de Schizosaccharomyces pombe/genética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Subunits); 0 (Recombinant Proteins); 0 (Schizosaccharomyces pombe Proteins); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (NatA protein, S pombe)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171011
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186278


  9 / 8416 MEDLINE  
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[PMID]:28943298
[Au] Autor:Kabeya N; Chiba M; Haga Y; Satoh S; Yoshizaki G
[Ad] Endereço:Department of Aquatic Bioscience, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1, Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
[Ti] Título:Cloning and functional characterization of fads2 desaturase and elovl5 elongase from Japanese flounder Paralichthys olivaceus.
[So] Source:Comp Biochem Physiol B Biochem Mol Biol;214:36-46, 2017 Dec.
[Is] ISSN:1879-1107
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Japanese flounder Paralichthys olivaceus has an essential requirement for long-chain polyunsaturated fatty acids (LC-PUFA), particularly docosahexaenoic acid and eicosapentaenoic acid, but the enzymes involved in LC-PUFA biosynthesis are thought to be absent or to have low activity. Teleost fish, in particular, have quite diversified substrate preference of these enzymes even among closely related species, implying that each species could have different LC-PUFA biosynthetic capabilities. Therefore, in the present study, we characterized Japanese flounder fatty acid desaturase 2 (Fads2) and elongation of very long-chain fatty acids protein 5 (Elovl5) in order to precisely characterize the LC-PUFA biosynthesis pathway. Fads2 has Δ6 and Δ8 desaturase activity and Elovl5 has elongase activity toward C18 and C20 PUFA, suggesting that Japanese flounder is capable of synthesizing 20:4n-3 and 20:3n-6 from 18:3n-3 and 18:2n-6, respectively. Expression analysis showed that the fads2 was highly expressed in the brain and eye, while the elovl5 was highly expressed in the eye and pyloric caeca. This information will be beneficial for developing an ideal feed to support the aquaculture of Japanese flounder.
[Mh] Termos MeSH primário: Acetiltransferases/genética
Ácidos Graxos Dessaturases/genética
Ácidos Graxos Insaturados/metabolismo
Proteínas de Peixes/genética
Linguado/genética
[Mh] Termos MeSH secundário: Acetiltransferases/metabolismo
Sequência de Aminoácidos
Animais
Sítios de Ligação
Encéfalo/metabolismo
Ceco/metabolismo
Clonagem Molecular
Olho/metabolismo
Ácidos Graxos Dessaturases/metabolismo
Proteínas de Peixes/metabolismo
Linguado/classificação
Linguado/metabolismo
Expressão Gênica
Cinética
Especificidade de Órgãos
Filogenia
Pichia/genética
Pichia/metabolismo
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids, Unsaturated); 0 (Fish Proteins); 0 (Recombinant Proteins); EC 1.14.19.- (Fatty Acid Desaturases); EC 2.3.1.- (Acetyltransferases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170926
[St] Status:MEDLINE


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[PMID]:28934466
[Au] Autor:Lu Y; Dai X; Zhang M; Miao Y; Zhou C; Cui Z; Xiong B
[Ad] Endereço:College of Animal Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
[Ti] Título:Cohesin acetyltransferase Esco2 regulates SAC and kinetochore functions via maintaining H4K16 acetylation during mouse oocyte meiosis.
[So] Source:Nucleic Acids Res;45(16):9388-9397, 2017 Sep 19.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Sister chromatid cohesion, mediated by cohesin complex and established by the acetyltransferases Esco1 and Esco2, is essential for faithful chromosome segregation. Mutations in Esco2 cause Roberts syndrome, a developmental disease characterized by severe prenatal retardation as well as limb and facial abnormalities. However, its exact roles during oocyte meiosis have not clearly defined. Here, we report that Esco2 localizes to the chromosomes during oocyte meiotic maturation. Depletion of Esco2 by morpholino microinjection leads to the precocious polar body extrusion, the escape of metaphase I arrest induced by nocodazole treatment and the loss of BubR1 from kinetochores, indicative of inactivated SAC. Furthermore, depletion of Esco2 causes a severely impaired spindle assembly and chromosome alignment, accompanied by the remarkably elevated incidence of defective kinetochore-microtubule attachments which consequently lead to the generation of aneuploid eggs. Notably, we find that the involvement of Esco2 in SAC and kinetochore functions is mediated by its binding to histone H4 and acetylation of H4K16 both in vivo and in vitro. Thus, our data assign a novel meiotic function to Esco2 beyond its role in the cohesion establishment during mouse oocyte meiosis.
[Mh] Termos MeSH primário: Acetiltransferases/metabolismo
Histonas/metabolismo
Cinetocoros/metabolismo
Pontos de Checagem da Fase M do Ciclo Celular/genética
Meiose/genética
Oócitos/enzimologia
[Mh] Termos MeSH secundário: Acetilação
Acetiltransferases/fisiologia
Aneuploidia
Animais
Cromossomos de Mamíferos/enzimologia
Feminino
Histonas/química
Lisina/metabolismo
Camundongos Endogâmicos ICR
Fuso Acromático/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histones); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (establishment of cohesion 1 homolog 2, mouse); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx563



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