Base de dados : MEDLINE
Pesquisa : D08.811.913.050.134.415.500.074 [Categoria DeCS]
Referências encontradas : 9 [refinar]
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  1 / 9 MEDLINE  
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[PMID]:27799288
[Au] Autor:Molina-Serrano D; Schiza V; Demosthenous C; Stavrou E; Oppelt J; Kyriakou D; Liu W; Zisser G; Bergler H; Dang W; Kirmizis A
[Ad] Endereço:Department of Biological Sciences, University of Cyprus, Nicosia, Cyprus.
[Ti] Título:Loss of Nat4 and its associated histone H4 N-terminal acetylation mediates calorie restriction-induced longevity.
[So] Source:EMBO Rep;17(12):1829-1843, 2016 Dec.
[Is] ISSN:1469-3178
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Changes in histone modifications are an attractive model through which environmental signals, such as diet, could be integrated in the cell for regulating its lifespan. However, evidence linking dietary interventions with specific alterations in histone modifications that subsequently affect lifespan remains elusive. We show here that deletion of histone N-alpha-terminal acetyltransferase Nat4 and loss of its associated H4 N-terminal acetylation (N-acH4) extend yeast replicative lifespan. Notably, nat4Δ-induced longevity is epistatic to the effects of calorie restriction (CR). Consistent with this, (i) Nat4 expression is downregulated and the levels of N-acH4 within chromatin are reduced upon CR, (ii) constitutive expression of Nat4 and maintenance of N-acH4 levels reduces the extension of lifespan mediated by CR, and (iii) transcriptome analysis indicates that nat4Δ largely mimics the effects of CR, especially in the induction of stress-response genes. We further show that nicotinamidase Pnc1, which is typically upregulated under CR, is required for nat4Δ-mediated longevity. Collectively, these findings establish histone N-acH4 as a regulator of cellular lifespan that links CR to increased stress resistance and longevity.
[Mh] Termos MeSH primário: Restrição Calórica
Regulação Fúngica da Expressão Gênica
Histonas/metabolismo
Acetiltransferase N-Terminal D/deficiência
Acetiltransferase N-Terminal D/fisiologia
Proteínas de Saccharomyces cerevisiae/fisiologia
Saccharomyces cerevisiae/fisiologia
[Mh] Termos MeSH secundário: Acetilação
Cromatina/metabolismo
Regulação para Baixo
Perfilação da Expressão Gênica
Histona Acetiltransferases/metabolismo
Longevidade
Acetiltransferase N-Terminal D/genética
Nicotinamidase/genética
Nicotinamidase/metabolismo
Processamento de Proteína Pós-Traducional
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Fatores de Tempo
Ativação Transcricional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (Histones); 0 (Saccharomyces cerevisiae Proteins); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.88 (N-Terminal Acetyltransferase D); EC 2.3.1.88 (NAT4 protein, S cerevisiae); EC 3.5.1.19 (Nicotinamidase); EC 3.5.1.19 (PNC1 protein, S cerevisiae)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161102
[St] Status:MEDLINE


  2 / 9 MEDLINE  
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[PMID]:26666750
[Au] Autor:Pavlou D; Kirmizis A
[Ad] Endereço:Department of Biological Sciences, University of Cyprus, Nicosia, Cyprus.
[Ti] Título:Depletion of histone N-terminal-acetyltransferase Naa40 induces p53-independent apoptosis in colorectal cancer cells via the mitochondrial pathway.
[So] Source:Apoptosis;21(3):298-311, 2016 Mar.
[Is] ISSN:1573-675X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Protein N-terminal acetylation is an abundant post-translational modification in eukaryotes implicated in various fundamental cellular and biochemical processes. This modification is catalysed by evolutionarily conserved N-terminal acetyltransferases (NATs) whose deregulation has been linked to cancer development and thus, are emerging as useful diagnostic and therapeutic targets. Naa40 is a highly selective NAT that acetylates the amino-termini of histones H4 and H2A and acts as a sensor of cell growth in yeast. In the present study, we examine the role of Naa40 in cancer cell survival. We demonstrate that depletion of Naa40 in HCT116 and HT-29 colorectal cancer cells decreases cell survival by enhancing apoptosis, whereas Naa40 reduction in non-cancerous mouse embryonic fibroblasts has no effect on cell viability. Specifically, Naa40 knockdown in colon cancer cells activates the mitochondrial caspase-9-mediated apoptotic cascade. Consistent with this, we show that caspase-9 activation is required for the induced apoptosis because treatment of cells with an irreversible caspase-9 inhibitor impedes apoptosis when Naa40 is depleted. Furthermore, the effect of Naa40-depletion on cell-death is mediated through a p53-independent mechanism since p53-null HCT116 cells still undergo apoptosis upon reduction of the acetyltransferase. Altogether, these findings reveal an anti-apoptotic role for Naa40 and exhibit its potential as a therapeutic target in colorectal cancers.
[Mh] Termos MeSH primário: Apoptose/genética
Carcinogênese/genética
Caspase 9/metabolismo
Neoplasias Colorretais/genética
Mitocôndrias/metabolismo
Acetiltransferase N-Terminal D/fisiologia
Proteína Supressora de Tumor p53/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Animais
Inibidores de Caspase/farmacologia
Sobrevivência Celular
Neoplasias Colorretais/patologia
Técnicas de Silenciamento de Genes
Células HCT116
Células HT29
Histonas/metabolismo
Seres Humanos
Camundongos
Acetiltransferase N-Terminal D/genética
Processamento de Proteína Pós-Traducional/genética
RNA Interferente Pequeno/genética
Transdução de Sinais
Proteína Supressora de Tumor p53/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caspase Inhibitors); 0 (Histones); 0 (RNA, Small Interfering); 0 (TP53 protein, human); 0 (Tumor Suppressor Protein p53); EC 2.3.1.88 (N-Terminal Acetyltransferase D); EC 2.3.1.88 (NAA40 protein, human); EC 3.4.22.- (CASP9 protein, human); EC 3.4.22.- (Caspase 9)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151216
[St] Status:MEDLINE
[do] DOI:10.1007/s10495-015-1207-0


  3 / 9 MEDLINE  
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[PMID]:25886145
[Au] Autor:Van Damme P; Hole K; Gevaert K; Arnesen T
[Ad] Endereço:Department of Medical Protein Research, VIB, Ghent, Belgium.
[Ti] Título:N-terminal acetylome analysis reveals the specificity of Naa50 (Nat5) and suggests a kinetic competition between N-terminal acetyltransferases and methionine aminopeptidases.
[So] Source:Proteomics;15(14):2436-46, 2015 Jul.
[Is] ISSN:1615-9861
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Cotranslational N-terminal (Nt-) acetylation of nascent polypeptides is mediated by N-terminal acetyltransferases (NATs). The very N-terminal amino acid sequence largely determines whether or not a given protein is Nt-acetylated. Currently, there are six distinct NATs characterized, NatA-NatF, in humans of which the in vivo substrate specificity of Naa50 (Nat5)/NatE, an alternative catalytic subunit of the human NatA, so far remained elusive. In this study, we quantitatively compared the Nt-acetylomes of wild-type yeast S. cerevisiae expressing the endogenous yeast Naa50 (yNaa50), the congenic strain lacking yNaa50, and an otherwise identical strain expressing human Naa50 (hNaa50). Six canonical yeast NatA substrates were Nt-acetylated less in yeast lacking yNaa50 than in wild-type yeast. In contrast, the ectopically expressed hNaa50 resulted, predominantly, in the Nt-acetylation of N-terminal Met (iMet) starting N-termini, including iMet-Lys, iMet-Val, iMet-Ala, iMet-Tyr, iMet-Phe, iMet-Leu, iMet-Ser, and iMet-Thr N-termini. This identified hNaa50 as being similar, in its substrate specificity, to the previously characterized hNaa60/NatF. In addition, the identification, in yNaa50-lacking yeast expressing hNaa50, of Nt-acetylated iMet followed by a small residue such as Ser, Thr, Ala, or Val, revealed a kinetic competition between Naa50 and Met-aminopeptidases (MetAPs), and implied that Nt-acetylated iMet followed by a small residue cannot be removed by MetAPs, a deduction supported by our in vitro data. As such, Naa50-mediated Nt-acetylation may act to retain the iMet of proteins of otherwise MetAP susceptible N-termini and the fraction of retained and Nt-acetylated iMet (followed by a small residue) in such a setting would be expected to depend on the relative levels of ribosome-associated Naa50/NatA and MetAPs.
[Mh] Termos MeSH primário: Aminopeptidases/metabolismo
Glicoproteínas/metabolismo
Metionina/metabolismo
Acetiltransferase N-Terminal D/metabolismo
Acetiltransferase N-Terminal E/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Sequência de Aminoácidos
Aminopeptidases/química
Deleção de Genes
Expressão Gênica
Glicoproteínas/química
Seres Humanos
Cinética
Dados de Sequência Molecular
Acetiltransferase N-Terminal D/química
Acetiltransferase N-Terminal D/genética
Acetiltransferase N-Terminal E/química
Acetiltransferase N-Terminal E/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Saccharomyces cerevisiae/química
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Glycoproteins); 0 (Recombinant Proteins); 0 (Saccharomyces cerevisiae Proteins); AE28F7PNPL (Methionine); EC 2.3.1.88 (N-Terminal Acetyltransferase D); EC 2.3.1.88 (N-Terminal Acetyltransferase E); EC 2.3.1.88 (NAA50 protein, human); EC 2.3.1.88 (NAT5 protein, S cerevisiae); EC 3.4.11.- (Aminopeptidases); EC 3.4.11.18 (METAP2 protein, human)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:150716
[Lr] Data última revisão:
150716
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150418
[St] Status:MEDLINE
[do] DOI:10.1002/pmic.201400575


  4 / 9 MEDLINE  
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[PMID]:25619998
[Au] Autor:Magin RS; Liszczak GP; Marmorstein R
[Ad] Endereço:Department of Biochemistry and Biophysics, Abramson Family Cancer Research Institute, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104, USA; Program in Gene Expression and Regulation, The Wistar Institute, Philadelphia, PA 19104, USA; Graduate Group in Biochemistry and Biophysics, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104, USA.
[Ti] Título:The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD.
[So] Source:Structure;23(2):332-41, 2015 Feb 03.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:N-terminal acetylation is among the most common protein modifications in eukaryotes and is mediated by evolutionarily conserved N-terminal acetyltransferases (NATs). NatD is among the most selective NATs; its only known substrates are histones H4 and H2A, containing the N-terminal sequence SGRGK in humans. Here we characterize the molecular basis for substrate-specific acetylation by NatD by reporting its crystal structure bound to cognate substrates and performing related biochemical studies. A novel N-terminal segment wraps around the catalytic core domain to make stabilizing interactions, and the α1-α2 and ß6-ß7 loops adopt novel conformations to properly orient the histone N termini in the binding site. Ser1 and Arg3 of the histone make extensive contacts to highly conserved NatD residues in the substrate binding pocket, and flanking glycine residues also appear to contribute to substrate-specific binding by NatD, together defining a Ser-Gly-Arg-Gly recognition sequence. These studies have implications for understanding substrate-specific acetylation by NAT enzymes.
[Mh] Termos MeSH primário: Histonas/química
Acetiltransferase N-Terminal D/química
Schizosaccharomyces/enzimologia
[Mh] Termos MeSH secundário: Acetilação
Sequência de Aminoácidos
Histonas/metabolismo
Seres Humanos
Modelos Moleculares
Dados de Sequência Molecular
Acetiltransferase N-Terminal D/genética
Acetiltransferase N-Terminal D/metabolismo
Alinhamento de Sequência
Especificidade da Espécie
Eletricidade Estática
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Histones); EC 2.3.1.88 (N-Terminal Acetyltransferase D)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150127
[St] Status:MEDLINE


  5 / 9 MEDLINE  
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[PMID]:24248912
[Au] Autor:Jedrzejewski RP; Kazmierkiewicz R
[Ad] Endereço:Laboratory of Biomolecular Systems Simulations, Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Kladki 24, 80-822, Gdansk, Poland, rochjedrzejewski@gmail.com.
[Ti] Título:Structure of Patt1 human proapoptotic histone acetyltransferase.
[So] Source:J Mol Model;19(12):5533-8, 2013 Dec.
[Is] ISSN:0948-5023
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The results of modeling of a novel human histone acetyltransferase Patt1 are presented here. This protein belongs to the GNAT GCN5 family and shows proapoptotic activity in human hepatocellular carcinoma cells. Patt1 is an attractive therapeutic target. The sequence analysis, fold recognition predictions and homology modeling of Patt1 protein structure were performed. N- and C- termini of Patt1 were unstructured. Central part revealed classical GNAT fold-central 7-stranded beta sheet core surrounded by intervening 4 alpha helices. The model was assessed with the methods for protein structure validation PROQ and MetaMQAPII. The all-atom 12 ns molecular dynamics simulation of Patt1 model with TIP3P water model and counterions was conducted. All assessment methods implemented resulted in conviction that the model was of quality that could provide confident structural information to infer sequence-structure-function relationships of Patt1. Phe186 and Cys137 were identified as residues engaged in acetyltransfer reaction and the clues for the identification of reaction mechanism were proposed. The knowledge of detailed molecular architecture of Patt1 is not only the key to understanding its mechanistic functional properties but it also opens the possibility of rational drug and protein design experiments, leading to development of effective therapeutic methods.
[Mh] Termos MeSH primário: Apoptose/genética
Carcinoma Hepatocelular/genética
Histona Acetiltransferases/química
Neoplasias Hepáticas/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Carcinoma Hepatocelular/química
Carcinoma Hepatocelular/patologia
Histona Acetiltransferases/genética
Seres Humanos
Neoplasias Hepáticas/química
Neoplasias Hepáticas/patologia
Simulação de Dinâmica Molecular
Acetiltransferase N-Terminal D
Conformação Proteica
Dobramento de Proteína
Estrutura Secundária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.88 (N-Terminal Acetyltransferase D); EC 2.3.1.88 (NAA40 protein, human)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:161128
[Lr] Data última revisão:
161128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131120
[St] Status:MEDLINE
[do] DOI:10.1007/s00894-013-2043-1


  6 / 9 MEDLINE  
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[PMID]:21935442
[Au] Autor:Hole K; Van Damme P; Dalva M; Aksnes H; Glomnes N; Varhaug JE; Lillehaug JR; Gevaert K; Arnesen T
[Ad] Endereço:Department of Molecular Biology, University of Bergen, Bergen, Norway.
[Ti] Título:The human N-alpha-acetyltransferase 40 (hNaa40p/hNatD) is conserved from yeast and N-terminally acetylates histones H2A and H4.
[So] Source:PLoS One;6(9):e24713, 2011.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein N(α)-terminal acetylation (Nt-acetylation) is considered one of the most common protein modification in eukaryotes, and 80-90% of all soluble human proteins are modified in this way, with functional implications ranging from altered protein function and stability to translocation potency amongst others. Nt-acetylation is catalyzed by N-terminal acetyltransferases (NATs), and in yeast five NAT types are identified and denoted NatA-NatE. Higher eukaryotes additionally express NatF. Except for NatD, human orthologues for all yeast NATs are identified. yNatD is defined as the catalytic unit Naa40p (Nat4) which co-translationally Nt-acetylates histones H2A and H4. In this study we identified and characterized hNaa40p/hNatD, the human orthologue of the yeast Naa40p. An in vitro proteome-derived peptide library Nt-acetylation assay indicated that recombinant hNaa40p acetylates N-termini starting with the consensus sequence Ser-Gly-Gly-Gly-Lys-, strongly resembling the N-termini of the human histones H2A and H4. This was confirmed as recombinant hNaa40p Nt-acetylated the oligopeptides derived from the N-termini of both histones. In contrast, a synthetically Nt-acetylated H4 N-terminal peptide with all lysines being non-acetylated, was not significantly acetylated by hNaa40p, indicating that hNaa40p catalyzed H4 N(α)-acetylation and not H4 lysine N(ε)-acetylation. Also, immunoprecipitated hNaa40p specifically Nt-acetylated H4 in vitro. Heterologous expression of hNaa40p in a yeast naa40-Δ strain restored Nt-acetylation of yeast histone H4, but not H2A in vivo, probably reflecting the fact that the N-terminal sequences of human H2A and H4 are highly similar to each other and to yeast H4 while the N-terminal sequence of yeast H2A differs. Thus, Naa40p seems to have co-evolved with the human H2A sequence. Finally, a partial co-sedimentation with ribosomes indicates that hNaa40p co-translationally acetylates H2A and H4. Combined, our results strongly suggest that human Naa40p/NatD is conserved from yeast. Thus, the NATs of all classes of N-terminally acetylated proteins in humans now appear to be accounted for.
[Mh] Termos MeSH primário: Acetiltransferases/química
Acetiltransferases/metabolismo
Histonas/metabolismo
Leveduras/enzimologia
[Mh] Termos MeSH secundário: Acetilação
Acetiltransferases/genética
Sequência de Aminoácidos
Seres Humanos
Imunoprecipitação
Dados de Sequência Molecular
Acetiltransferase N-Terminal D
Ligação Proteica
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Histones); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.88 (N-Terminal Acetyltransferase D); EC 2.3.1.88 (NAA40 protein, human)
[Em] Mês de entrada:1202
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110922
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0024713


  7 / 9 MEDLINE  
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[PMID]:19695338
[Au] Autor:Liu Z; Liu Y; Wang H; Ge X; Jin Q; Ding G; Hu Y; Zhou B; Chen Z; Ge X; Zhang B; Man X; Zhai Q
[Ad] Endereço:Key Laboratory of Nutrition and Metabolism, Institute for Nutritional Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, and Graduate School of the Chinese Academy of Sciences, 294 Taiyuan Road, Shanghai 200031, China.
[Ti] Título:Patt1, a novel protein acetyltransferase that is highly expressed in liver and downregulated in hepatocellular carcinoma, enhances apoptosis of hepatoma cells.
[So] Source:Int J Biochem Cell Biol;41(12):2528-37, 2009 Dec.
[Is] ISSN:1878-5875
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Protein acetylation is increasingly recognized as an important post-translational modification. Although a lot of protein acetyltransferases have been identified, a few putative acetyltransferases are yet to be studied. In this study, we identified a novel protein acetyltransferase, Patt1, which belongs to GNAT family. Patt1 exhibited histone acetyltransferase activity and auto-acetylation activity. Deletion and mutation analysis of the predicted acetyltransferase domain in Patt1 showed that the conserved Glu139 was an important residue for its protein acetyltransferase activity. Furthermore, we found that Patt1 was highly expressed in liver and significantly downregulated in hepatocellular carcinoma tissues. In addition, we showed that overexpression of Patt1 enhanced the apoptosis of hepatoma cells dependent on its acetyltransferase activity, whereas knockdown of Patt1 significantly protected Chang liver cells from apoptosis. These data suggest that Patt1 might be involved in the development of hepatocellular carcinoma, and could be served as a potential therapy target for hepatocellular carcinoma.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/enzimologia
Histona Acetiltransferases/metabolismo
Neoplasias Hepáticas Experimentais/enzimologia
Neoplasias Hepáticas/enzimologia
Fígado/enzimologia
[Mh] Termos MeSH secundário: Animais
Apoptose/genética
Carcinoma Hepatocelular/patologia
Clonagem Molecular
Regulação Neoplásica da Expressão Gênica
Células HeLa
Histona Acetiltransferases/genética
Seres Humanos
Fígado/patologia
Neoplasias Hepáticas/patologia
Neoplasias Hepáticas Experimentais/patologia
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Acetiltransferase N-Terminal D
RNA Interferente Pequeno/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Small Interfering); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.88 (N-Terminal Acetyltransferase D); EC 2.3.1.88 (NAA40 protein, human)
[Em] Mês de entrada:1006
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090822
[St] Status:MEDLINE
[do] DOI:10.1016/j.biocel.2009.08.009


  8 / 9 MEDLINE  
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[PMID]:19332560
[Au] Autor:Polevoda B; Hoskins J; Sherman F
[Ad] Endereço:Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, NY 14642, USA.
[Ti] Título:Properties of Nat4, an N(alpha)-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4.
[So] Source:Mol Cell Biol;29(11):2913-24, 2009 Jun.
[Is] ISSN:1098-5549
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nat4, also designated NatD, was previously shown to acetylate the N termini of histones H2A and H4, which have SGGKG and SGRGK N termini (O. K. Song, X. Wang, J. H. Waterborg, and R. Sternglanz, J. Biol. Chem. 278:38109-38112, 2003). The analysis of chimeric proteins with various N-terminal segments of histone H4 fused to iso-1-cytochrome c revealed that efficient acetylation by NatD required at least 30 to 50 amino acid residues of the N terminus of histone H4. This requirement for an extended N terminus is in marked contrast with the major N-terminal acetyl transferases (NATs), i.e., NatA, NatB, and NatC, which require as few as two specific residues and usually no more than four or five. However, similar to the other NATs, NatD is associated with ribosomes. The nat4-Delta strain showed several minor phenotypes, including sensitivity to 3-aminotriazole, benomyl, and thiabendazole. Moreover, these nat4-Delta phenotypes were enhanced in the strain containing K5R K8R K12R replacements in the N-tail of histone H4, suggesting that the lack of N-terminal serine acetylation is synergistic to the lack of acetylation of the H4 N-tail lysines. Thus, N-terminal serine acetylation of histone H4 may be a part of an essential charge patch first described for the histone H2A.Z variant in Tetrahymena species.
[Mh] Termos MeSH primário: Acetiltransferases/metabolismo
Histonas/química
Histonas/metabolismo
Processamento de Proteína Pós-Traducional
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
[Mh] Termos MeSH secundário: Acetilação
Alelos
Sequência de Aminoácidos
Centrifugação com Gradiente de Concentração
Citocromos c/química
Citocromos c/metabolismo
Histona Acetiltransferases
Dados de Sequência Molecular
Mutação/genética
Acetiltransferase N-Terminal D
Fenótipo
Polirribossomos/enzimologia
Estrutura Secundária de Proteína
Transporte Proteico
Proteínas Recombinantes de Fusão/metabolismo
Saccharomyces cerevisiae/citologia
Proteínas de Saccharomyces cerevisiae/química
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (CYC1 protein, S cerevisiae); 0 (Histones); 0 (Recombinant Fusion Proteins); 0 (Saccharomyces cerevisiae Proteins); 9007-43-6 (Cytochromes c); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.88 (N-Terminal Acetyltransferase D); EC 2.3.1.88 (NAT4 protein, S cerevisiae)
[Em] Mês de entrada:0906
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090401
[St] Status:MEDLINE
[do] DOI:10.1128/MCB.00147-08


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[PMID]:12915400
[Au] Autor:Song OK; Wang X; Waterborg JH; Sternglanz R
[Ad] Endereço:Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 11794-5215, USA.
[Ti] Título:An Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A.
[So] Source:J Biol Chem;278(40):38109-12, 2003 Oct 03.
[Is] ISSN:0021-9258
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A yeast gene has been identified that encodes a novel, evolutionarily conserved Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A. The gene has been named NAT4. Recombinant Nat4 protein acetylated a peptide corresponding to the N-terminal tail of H4, but not an H3 peptide nor the peptide adrenocorticotropin. H4 and H2A are N-terminally acetylated in all species from yeast to mammals and hence blocked from sequencing by Edman degradation. In contrast, H4 and H2A purified from a nat4 mutant were unacetylated and could be sequenced. Analysis of yeast histones by acid-urea gel electrophoresis showed that all the H4 and H2A from the mutant migrated more rapidly than the same histones from a wild type strain, consistent with the histones from the mutant having one extra positive charge due to one less acetylated amino group. A comparison of yeast proteins from wild type and a nat4 mutant by two-dimensional gel electrophoresis showed no evidence that other yeast proteins are substrates of this acetyltransferase. Thus, Nat4 may be dedicated specifically to the N-terminal acetylation of histones H4 and H2A. Surprisingly, nat4 mutants grow at a normal rate and have no readily observable phenotypes.
[Mh] Termos MeSH primário: Acetiltransferases/química
Acetiltransferases/metabolismo
Acetiltransferases/fisiologia
Histonas/química
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/fisiologia
[Mh] Termos MeSH secundário: Hormônio Adrenocorticotrópico/química
Motivos de Aminoácidos
Sequência de Aminoácidos
Sequência Conservada
Eletroforese em Gel Bidimensional
Eletroforese em Gel de Poliacrilamida
Histona Acetiltransferases
Histonas/metabolismo
Dados de Sequência Molecular
Mutação
Acetiltransferase N-Terminal D
Peptídeos/química
Fenótipo
Plasmídeos/metabolismo
Ligação Proteica
Estrutura Terciária de Proteína
Proteínas Recombinantes/química
Saccharomyces cerevisiae/metabolismo
Ureia/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Histones); 0 (Peptides); 0 (Recombinant Proteins); 0 (Saccharomyces cerevisiae Proteins); 8W8T17847W (Urea); 9002-60-2 (Adrenocorticotropic Hormone); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.88 (N-Terminal Acetyltransferase D); EC 2.3.1.88 (NAT4 protein, S cerevisiae)
[Em] Mês de entrada:0311
[Cu] Atualização por classe:161124
[Lr] Data última revisão:
161124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:030814
[St] Status:MEDLINE



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