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Pesquisa : D08.811.913.050.134.423 [Categoria DeCS]
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[PMID]:29247799
[Au] Autor:Varland S; Myklebust LM; Goksøyr SØ; Glomnes N; Torsvik J; Varhaug JE; Arnesen T
[Ad] Endereço:Department of Molecular Biology, University of Bergen, Thormøhlensgate 55, 5006 Bergen, Norway.
[Ti] Título:Identification of an alternatively spliced nuclear isoform of human N-terminal acetyltransferase Naa30.
[So] Source:Gene;644:27-37, 2018 Feb 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:N-terminal acetylation is a highly abundant and important protein modification in eukaryotes catalyzed by N-terminal acetyltransferases (NATs). In humans, six different NATs have been identified (NatA-NatF), each composed of individual subunits and acetylating a distinct set of substrates. Along with most NATs, NatC acts co-translationally at the ribosome. The NatC complex consists of the catalytic subunit Naa30 and the auxiliary subunits Naa35 and Naa38, and can potentially Nt-acetylate cytoplasmic proteins when the initiator methionine is followed by a bulky hydrophobic/amphipathic residue at position 2. Here, we have identified a splice variant of human NAA30, which encodes a truncated protein named Naa30 . The splice variant was abundantly present in thyroid cancer tissues and in several different human cancer cell lines. Surprisingly, Naa30 localized predominantly to the nucleus, as opposed to annotated Naa30 which has a cytoplasmic localization. Full-length Naa30 acetylated a classical NatC substrate peptide in vitro, whereas no significant NAT activity was detected for Naa30 Due to the nuclear localization, we also examined acetyltransferase activity towards lysine residues. Neither full-length Naa30 nor Naa30 displayed any lysine acetyltransferase activity. Overexpression of full-length Naa30 increased cell viability via inhibition of apoptosis. In contrast, Naa30 did not exert an anti-apoptotic effect. In sum, we identified a novel and widely expressed Naa30 isoform with a potential non-catalytic role in the nucleus.
[Mh] Termos MeSH primário: Núcleo Celular/genética
Acetiltransferase N-Terminal C/genética
Acetiltransferases N-Terminal/genética
Isoformas de Proteínas/genética
Processamento de RNA/genética
[Mh] Termos MeSH secundário: Acetilação
Sequência de Aminoácidos
Linhagem Celular
Linhagem Celular Tumoral
Sobrevivência Celular/genética
Células HEK293
Células HeLa
Seres Humanos
Lisina/genética
Células MCF-7
Processamento de Proteína Pós-Traducional/genética
Ribossomos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Isoforms); EC 2.3.1.88 (N-Terminal Acetyltransferase C); EC 2.3.1.88 (N-Terminal Acetyltransferases); EC 2.3.1.88 (NAA30 protein, human); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180119
[Lr] Data última revisão:
180119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171217
[St] Status:MEDLINE


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[PMID]:27385766
[Au] Autor:Feng J; Li R; Yu J; Ma S; Wu C; Li Y; Cao Y; Ma L
[Ad] Endereço:College of Life Sciences, Capital Normal University, and Key Laboratory of Plant Gene Resources and Biotechnology for Carbon Reduction and Environmental Improvement, Beijing Municipal Government; Beijing 100048, China.
[Ti] Título:Protein N-terminal acetylation is required for embryogenesis in Arabidopsis.
[So] Source:J Exp Bot;67(15):4779-89, 2016 Aug.
[Is] ISSN:1460-2431
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Early embryonic development generates precursors of all major cell types in Arabidopsis. Among these precursors, the hypophysis divides asymmetrically to form the progenitors of the quiescent center and columella stem cells. A great deal has been learnt about the mechanisms that control the asymmetric division of the hypophysis and embryogenesis at the transcriptional level; however, no evidence of regulation at the co- or post-translational level has been reported. Here, we show that mutation of the catalytic subunit (Naa10) or auxiliary subunit (Naa15) of NatA, an N-terminal acetyltransferase that catalyzes protein N-terminal acetylation, produces an embryo-lethal phenotype. In addition, Naa10 and Naa15 were found to interact physically in planta Further analysis revealed that the observed embryonic patterning defects started at the early globular stage and that the asymmetric division of the hypophysis was irregular; thus, no quiescent center progenitor cells were generated in naa10 and naa15 embryos. We further observed that the polar distributions of auxin and its efflux carrier PIN1 were disturbed in naa10 embryos. Our results suggest that NatA is required for asymmetric division of the hypophysis and early embryonic patterning in Arabidopsis, and provides a link between protein N-terminal acetylation and embryogenesis in plants.
[Mh] Termos MeSH primário: Arabidopsis/crescimento & desenvolvimento
Acetiltransferases N-Terminal/metabolismo
Sementes/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Acetilação
Arabidopsis/metabolismo
Imunoprecipitação
Acetiltransferases N-Terminal/fisiologia
Processamento de Proteína Pós-Traducional/fisiologia
Sementes/metabolismo
Técnicas do Sistema de Duplo-Híbrido
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.3.1.88 (N-Terminal Acetyltransferases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160708
[St] Status:MEDLINE
[do] DOI:10.1093/jxb/erw257


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[PMID]:27182737
[Au] Autor:Vetter AJ; Karamyshev AL; Patrick AE; Hudson H; Thomas PJ
[Ad] Endereço:Department of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas, United States of America.
[Ti] Título:N-Alpha-Acetyltransferases and Regulation of CFTR Expression.
[So] Source:PLoS One;11(5):e0155430, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The majority of cystic fibrosis (CF)-causing mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) lead to the misfolding, mistrafficking, and degradation of the mutant protein. Inhibition of degradation does not effectively increase the amount of trafficking competent CFTR, but typically leads to increased ER retention of misfolded forms. Thus, the initial off pathway steps occur early in the processing of the protein. To identify proteins that interact with these early forms of CFTR, in vitro crosslink experiments identified cotranslational partners of the nascent chain of the severe misfolded mutant, G85E CFTR. The mutant preferentially interacts with a subunit of an N-alpha-acetyltransferase A. Based on recent reports that acetylation of the N-termini of some N-end rule substrates control their ubiquitination and subsequent degradation, a potential role for this modification in regulation of CFTR expression was assessed. Knockdown experiments identified two complexes, which affect G85E CFTR proteins levels, NatA and NatB. Effects of the knockdowns on mRNA levels, translation rates, and degradation rates established that the two complexes regulate G85E CFTR through two separate mechanisms. NatA acts indirectly by regulating transcription levels and NatB acts through a previously identified, but incompletely understood posttranslational mechanism. This regulation did not effect trafficking of G85E CFTR, which remains retained in the ER, nor did it alter the degradation rate of CFTR. A mutation predicted to inhibit N-terminal acetylation of CFTR, Q2P, was without effect, suggesting neither system acts directly on CFTR. These results contradict the prediction that N-terminal acetylation of CFTR determines its fitness as a proteasome substrate, but rather NatB plays a role in the conformational maturation of CFTR in the ER through actions on an unidentified protein.
[Mh] Termos MeSH primário: Regulador de Condutância Transmembrana em Fibrose Cística/genética
Regulador de Condutância Transmembrana em Fibrose Cística/metabolismo
Regulação da Expressão Gênica
Acetiltransferases N-Terminal/metabolismo
[Mh] Termos MeSH secundário: Fibrose Cística/genética
Fibrose Cística/metabolismo
Regulador de Condutância Transmembrana em Fibrose Cística/química
Complexos Multiproteicos/metabolismo
Mutação
Ligação Proteica
Biossíntese de Proteínas
Domínios e Motivos de Interação entre Proteínas
Processamento de Proteína Pós-Traducional
Proteólise
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Multiprotein Complexes); 0 (RNA, Messenger); 126880-72-6 (Cystic Fibrosis Transmembrane Conductance Regulator); EC 2.3.1.88 (N-Terminal Acetyltransferases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170707
[Lr] Data última revisão:
170707
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160517
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0155430


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[PMID]:26861501
[Au] Autor:Rathore OS; Faustino A; Prudêncio P; Van Damme P; Cox CJ; Martinho RG
[Ad] Endereço:Department of Biomedical Sciences and Medicine, Faro, Portugal.
[Ti] Título:Absence of N-terminal acetyltransferase diversification during evolution of eukaryotic organisms.
[So] Source:Sci Rep;6:21304, 2016 Feb 10.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Protein N-terminal acetylation is an ancient and ubiquitous co-translational modification catalyzed by a highly conserved family of N-terminal acetyltransferases (NATs). Prokaryotes have at least 3 NATs, whereas humans have six distinct but highly conserved NATs, suggesting an increase in regulatory complexity of this modification during eukaryotic evolution. Despite this, and against our initial expectations, we determined that NAT diversification did not occur in the eukaryotes, as all six major human NATs were most likely present in the Last Eukaryotic Common Ancestor (LECA). Furthermore, we also observed that some NATs were actually secondarily lost during evolution of major eukaryotic lineages; therefore, the increased complexity of the higher eukaryotic proteome occurred without a concomitant diversification of NAT complexes.
[Mh] Termos MeSH primário: Arabidopsis/enzimologia
Evolução Biológica
Drosophila melanogaster/enzimologia
Células Eucarióticas/enzimologia
Acetiltransferases N-Terminal/genética
Saccharomyces cerevisiae/enzimologia
[Mh] Termos MeSH secundário: Acetilação
Sequência de Aminoácidos
Animais
Arabidopsis/metabolismo
Drosophila melanogaster/metabolismo
Células Eucarióticas/metabolismo
Variação Genética
Seres Humanos
Proteoma/genética
Saccharomyces cerevisiae/metabolismo
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Proteome); EC 2.3.1.88 (N-Terminal Acetyltransferases)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160211
[St] Status:MEDLINE
[do] DOI:10.1038/srep21304


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[PMID]:26818562
[Au] Autor:Favrot L; Blanchard JS; Vergnolle O
[Ad] Endereço:Department of Biochemistry, Albert Einstein College of Medicine , 1300 Morris Park Avenue, Bronx, New York 10461, United States.
[Ti] Título:Bacterial GCN5-Related N-Acetyltransferases: From Resistance to Regulation.
[So] Source:Biochemistry;55(7):989-1002, 2016 Feb 23.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes. Acetylation appears as a major regulatory post-translational modification and is as widespread as phosphorylation. N-Acetyltransferases transfer an acetyl group from acetyl-CoA to a large array of substrates, from small molecules such as aminoglycoside antibiotics to macromolecules. Acetylation of proteins can occur at two different positions, either at the amino-terminal end (αN-acetylation) or at the ε-amino group (εN-acetylation) of an internal lysine residue. GNAT members have been classified into different groups on the basis of their substrate specificity, and in spite of a very low primary sequence identity, GNAT proteins display a common and conserved fold. This Current Topic reviews the different classes of bacterial GNAT proteins, their functions, their structural characteristics, and their mechanism of action.
[Mh] Termos MeSH primário: Acetiltransferases/metabolismo
Aminoglicosídeos/metabolismo
Antibacterianos/metabolismo
Proteínas de Bactérias/metabolismo
Parede Celular/metabolismo
Farmacorresistência Bacteriana
Modelos Moleculares
[Mh] Termos MeSH secundário: Acetilação
Acetiltransferases/química
Acetiltransferases/classificação
Aminoaciltransferases/química
Aminoaciltransferases/classificação
Aminoaciltransferases/metabolismo
Aminoglicosídeos/farmacologia
Antibacterianos/farmacologia
Proteínas de Bactérias/química
Proteínas de Bactérias/classificação
Histona Acetiltransferases/química
Histona Acetiltransferases/metabolismo
Acetiltransferases N-Terminal/química
Acetiltransferases N-Terminal/classificação
Acetiltransferases N-Terminal/metabolismo
Conformação Proteica
Processamento de Proteína Pós-Traducional
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
0 (Aminoglycosides); 0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (FemA protein, Bacteria); 0 (Saccharomyces cerevisiae Proteins); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (N-epsilon-hydroxylysine acetyltransferase); EC 2.3.1.- (aminoglycoside acetyltransferase); EC 2.3.1.48 (GCN5 protein, S cerevisiae); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.88 (N-Terminal Acetyltransferases); EC 2.3.2.- (Aminoacyltransferases)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160129
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.5b01269


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[PMID]:26657068
[Au] Autor:Ma C; Pathak C; Lee SJ; Lee KY; Jang SB; Nam M; Im H; Yoon HJ; Lee BJ
[Ad] Endereço:Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Gwanak-gu, Seoul 151-742, Republic of Korea.
[Ti] Título:Alba from Thermoplasma volcanium belongs to α-NAT's: An insight into the structural aspects of Tv Alba and its acetylation by Tv Ard1.
[So] Source:Arch Biochem Biophys;590:90-100, 2016 Jan 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Alba superfamily proteins have been regarded as a conserved group of proteins in archaea and eukarya, which have shown to be important in nucleic acid binding, chromatic organization and gene regulation. These proteins often belong to the N-acetyltransferase (NAT) category (N(α)-acetyltransferases or N(ε)-acetyltransferases) and undergo post-translational modifications. Here, we report the crystal structure of Alba from Thermoplasma volcanium (Tv Alba) at 2.4 Å resolution. The acetylation of Tv Alba was monitored and the N-terminal of Tv Alba has been shown to interact with acetyl coenzyme A (Ac-CoA). The chemical shift perturbation experiments of Tv Alba were performed in the presence of Ac-CoA and/or Tv Ard1, another T. volcanium protein that treats Tv Alba as a substrate. To examine the DNA binding capabilities of Tv Alba alone and in the presence of Ac-CoA and/or Tv Ard1, EMSA experiments were carried out. It is shown that although Tv Alba binds to Ac-CoA, the acetylation of Tv Alba is not related with its binding to dsDNA, and the involvement of the N-terminus in Ac-CoA binding demonstrates that Tv Alba belongs to the N(α)-acetyltransferase family.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Proteínas Arqueais/ultraestrutura
DNA/química
Acetiltransferases N-Terminal/química
Acetiltransferases N-Terminal/ultraestrutura
Thermoplasma/enzimologia
[Mh] Termos MeSH secundário: Acetilação
Sequência de Aminoácidos
Sítios de Ligação
DNA/ultraestrutura
Dados de Sequência Molecular
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 9007-49-2 (DNA); EC 2.3.1.88 (N-Terminal Acetyltransferases)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170729
[Lr] Data última revisão:
170729
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151215
[St] Status:MEDLINE


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[PMID]:26522270
[Au] Autor:Casey JP; Støve SI; McGorrian C; Galvin J; Blenski M; Dunne A; Ennis S; Brett F; King MD; Arnesen T; Lynch SA
[Ad] Endereço:Clinical Genetics, Temple Street Children's University Hospital, Temple Street, Dublin 1, Ireland.
[Ti] Título:NAA10 mutation causing a novel intellectual disability syndrome with Long QT due to N-terminal acetyltransferase impairment.
[So] Source:Sci Rep;5:16022, 2015 Nov 02.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We report two brothers from a non-consanguineous Irish family presenting with a novel syndrome characterised by intellectual disability, facial dysmorphism, scoliosis and long QT. Their mother has a milder phenotype including long QT. X-linked inheritance was suspected. Whole exome sequencing identified a novel missense variant (c.128 A > C; p.Tyr43Ser) in NAA10 (X chromosome) as the cause of the family's disorder. Sanger sequencing confirmed that the mutation arose de novo in the carrier mother. NAA10 encodes the catalytic subunit of the major human N-terminal acetylation complex NatA. In vitro assays for the p.Tyr43Ser mutant enzyme showed a significant decrease in catalytic activity and reduced stability compared to wild-type Naa10 protein. NAA10 has previously been associated with Ogden syndrome, Lenz microphthalmia syndrome and non-syndromic developmental delay. Our findings expand the clinical spectrum of NAA10 and suggest that the proposed correlation between mutant Naa10 enzyme activity and phenotype severity is more complex than anticipated; the p.Tyr43Ser mutant enzyme has less catalytic activity than the p.Ser37Pro mutant associated with lethal Ogden syndrome but results in a milder phenotype. Importantly, we highlight the need for cardiac assessment in males and females with NAA10 variants as both patients and carriers can have long QT.
[Mh] Termos MeSH primário: Síndrome do QT Longo/genética
Acetiltransferase N-Terminal A/genética
Acetiltransferase N-Terminal E/genética
Polimorfismo de Nucleotídeo Único/genética
[Mh] Termos MeSH secundário: Adulto
Linhagem Celular Tumoral
Exoma/genética
Feminino
Células HeLa
Seres Humanos
Deficiência Intelectual/genética
Masculino
Acetiltransferases N-Terminal/genética
Fenótipo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 2.3.1.88 (N-Terminal Acetyltransferase A); EC 2.3.1.88 (N-Terminal Acetyltransferase E); EC 2.3.1.88 (N-Terminal Acetyltransferases); EC 2.3.1.88 (NAA10 protein, human)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151103
[St] Status:MEDLINE
[do] DOI:10.1038/srep16022


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[PMID]:26319188
[Au] Autor:Gibbs DJ
[Ad] Endereço:School of Biosciences, University of Birmingham, Edgbaston, B15 2TT, UK. Electronic address: d.gibbs@bham.ac.uk.
[Ti] Título:Emerging Functions for N-Terminal Protein Acetylation in Plants.
[So] Source:Trends Plant Sci;20(10):599-601, 2015 Oct.
[Is] ISSN:1878-4372
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:N-terminal (Nt-) acetylation is a widespread but poorly understood co-translational protein modification. Two reports now shed light onto the proteome-wide dynamics and protein-specific consequences of Nt-acetylation in relation to plant development, stress-response, and protein stability, identifying this modification as a key regulator of diverse aspects of plant growth and behaviour.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/enzimologia
Acetiltransferases N-Terminal/metabolismo
[Pt] Tipo de publicação:COMMENT; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); EC 2.3.1.88 (N-Terminal Acetyltransferases)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150831
[St] Status:MEDLINE


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[PMID]:25966763
[Au] Autor:Xu F; Huang Y; Li L; Gannon P; Linster E; Huber M; Kapos P; Bienvenut W; Polevoda B; Meinnel T; Hell R; Giglione C; Zhang Y; Wirtz M; Chen S; Li X
[Ad] Endereço:Michael Smith Laboratories, University of British Columbia, British Columbia V6T 1Z4, Canada Department of Botany, University of British Columbia, British Columbia V6T 1Z4, Canada.
[Ti] Título:Two N-terminal acetyltransferases antagonistically regulate the stability of a nod-like receptor in Arabidopsis.
[So] Source:Plant Cell;27(5):1547-62, 2015 May.
[Is] ISSN:1532-298X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nod-like receptors (NLRs) serve as immune receptors in plants and animals. The stability of NLRs is tightly regulated, though its mechanism is not well understood. Here, we show the crucial impact of N-terminal acetylation on the turnover of one plant NLR, Suppressor of NPR1, Constitutive 1 (SNC1), in Arabidopsis thaliana. Genetic and biochemical analyses of SNC1 uncovered its multilayered regulation by different N-terminal acetyltransferase (Nat) complexes. SNC1 exhibits a few distinct N-terminal isoforms generated through alternative initiation and N-terminal acetylation. Its first Met is acetylated by N-terminal acetyltransferase complex A (NatA), while the second Met is acetylated by N-terminal acetyltransferase complex B (NatB). Unexpectedly, the NatA-mediated acetylation serves as a degradation signal, while NatB-mediated acetylation stabilizes the NLR protein, thus revealing antagonistic N-terminal acetylation of a single protein substrate. Moreover, NatA also contributes to the turnover of another NLR, RESISTANCE TO P. syringae pv maculicola 1. The intricate regulation of protein stability by Nats is speculated to provide flexibility for the target protein in maintaining its homeostasis.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/enzimologia
Acetiltransferases N-Terminal/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Sequência de Aminoácidos
Arabidopsis/genética
Proteínas de Arabidopsis/genética
Mapeamento Cromossômico
Clonagem Molecular
Modelos Biológicos
Dados de Sequência Molecular
Mutação
Acetiltransferases N-Terminal/genética
Estabilidade Proteica
Plântulas/enzimologia
Plântulas/genética
Alinhamento de Sequência
Tabaco/enzimologia
Tabaco/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (SNC1 protein, Arabidopsis); EC 2.3.1.88 (N-Terminal Acetyltransferases)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:160501
[Lr] Data última revisão:
160501
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150514
[St] Status:MEDLINE
[do] DOI:10.1105/tpc.15.00173


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[PMID]:25951519
[Au] Autor:Dinh TV; Bienvenut WV; Linster E; Feldman-Salit A; Jung VA; Meinnel T; Hell R; Giglione C; Wirtz M
[Ad] Endereço:Department of Plant Molecular Biology, Centre for Organismal Studies, University of Heidelberg, Heidelberg, Germany.
[Ti] Título:Molecular identification and functional characterization of the first Nα-acetyltransferase in plastids by global acetylome profiling.
[So] Source:Proteomics;15(14):2426-35, 2015 Jul.
[Is] ISSN:1615-9861
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Protein N(α) -terminal acetylation represents one of the most abundant protein modifications of higher eukaryotes. In humans, six N(α) -acetyltransferases (Nats) are responsible for the acetylation of approximately 80% of the cytosolic proteins. N-terminal protein acetylation has not been evidenced in organelles of metazoans, but in higher plants is a widespread modification not only in the cytosol but also in the chloroplast. In this study, we identify and characterize the first organellar-localized Nat in eukaryotes. A primary sequence-based search in Arabidopsis thaliana revealed seven putatively plastid-localized Nats of which AT2G39000 (AtNAA70) showed the highest conservation of the acetyl-CoA binding pocket. The chloroplastic localization of AtNAA70 was demonstrated by transient expression of AtNAA70:YFP in Arabidopsis mesophyll protoplasts. Homology modeling uncovered a significant conservation of tertiary structural elements between human HsNAA50 and AtNAA70. The in vivo acetylation activity of AtNAA70 was demonstrated on a number of distinct protein N(α) -termini with a newly established global acetylome profiling test after expression of AtNAA70 in E. coli. AtNAA70 predominately acetylated proteins starting with M, A, S and T, providing an explanation for most protein N-termini acetylation events found in chloroplasts. Like HsNAA50, AtNAA70 displays N(ε) -acetyltransferase activity on three internal lysine residues. All MS data have been deposited in the ProteomeXchange with identifier PXD001947 (http://proteomecentral.proteomexchange.org/dataset/PXD001947).
[Mh] Termos MeSH primário: Arabidopsis/enzimologia
Acetiltransferases N-Terminal/análise
Plastídeos/enzimologia
[Mh] Termos MeSH secundário: Acetilação
Sequência de Aminoácidos
Arabidopsis/genética
Arabidopsis/metabolismo
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Seres Humanos
Modelos Moleculares
Dados de Sequência Molecular
Acetiltransferases N-Terminal/genética
Acetiltransferases N-Terminal/metabolismo
Plastídeos/genética
Plastídeos/metabolismo
Conformação Proteica
Proteômica
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 2.3.1.88 (N-Terminal Acetyltransferases)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150508
[St] Status:MEDLINE
[do] DOI:10.1002/pmic.201500025



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