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Pesquisa : D08.811.913.050.134.423.200 [Categoria DeCS]
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  1 / 24 MEDLINE  
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[PMID]:28380339
[Au] Autor:Hong H; Cai Y; Zhang S; Ding H; Wang H; Han A
[Ad] Endereço:State Key Laboratory for Cellular Stress Biology, Department of Biomedical Sciences, School of Life Sciences, Xiamen University, Xiang'an, Xiamen 361102, China.
[Ti] Título:Molecular Basis of Substrate Specific Acetylation by N-Terminal Acetyltransferase NatB.
[So] Source:Structure;25(4):641-649.e3, 2017 Apr 04.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The NatB N-terminal acetyltransferase specifically acetylates the N-terminal group of substrate protein peptides starting with Met-Asp/Glu/Asn/Gln. How NatB recognizes and acetylates these substrates remains unknown. Here, we report crystal structures of a NatB holoenzyme from Candida albicans in the presence of its co-factor CoA and substrate peptides. The auxiliary subunit Naa25 of NatB forms a horseshoe-like deck to hold specifically its catalytic subunit Naa20. The first two amino acids Met and Asp of a substrate peptide mediate the major interactions with the active site in the Naa20 subunit. The hydrogen bonds between the substrate Asp and pocket residues of Naa20 are essential to determine the NatB substrate specificity. Moreover, a hydrogen bond between the amino group of the substrate Met and a carbonyl group in the Naa20 active site directly anchors the substrate toward acetyl-CoA. Together, these structures define a unique molecular mechanism of specific N-terminal acetylation acted by NatB.
[Mh] Termos MeSH primário: Candida albicans/enzimologia
Acetiltransferase N-Terminal B/química
Acetiltransferase N-Terminal B/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Sítios de Ligação
Candida albicans/química
Domínio Catalítico
Ligações de Hidrogênio
Modelos Moleculares
Ligação Proteica
Multimerização Proteica
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.3.1.88 (N-Terminal Acetyltransferase B)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170406
[St] Status:MEDLINE


  2 / 24 MEDLINE  
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[PMID]:27881602
[Au] Autor:Gao J; Barroso C; Zhang P; Kim HM; Li S; Labrador L; Lightfoot J; Gerashchenko MV; Labunskyy VM; Dong MQ; Martinez-Perez E; Colaiácovo MP
[Ad] Endereço:Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA.
[Ti] Título:N-terminal acetylation promotes synaptonemal complex assembly in C. elegans.
[So] Source:Genes Dev;30(21):2404-2416, 2016 Nov 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:N-terminal acetylation of the first two amino acids on proteins is a prevalent cotranslational modification. Despite its abundance, the biological processes associated with this modification are not well understood. Here, we mapped the pattern of protein N-terminal acetylation in Caenorhabditis elegans, uncovering a conserved set of rules for this protein modification and identifying substrates for the N-terminal acetyltransferase B (NatB) complex. We observed an enrichment for global protein N-terminal acetylation and also specifically for NatB substrates in the nucleus, supporting the importance of this modification for regulating biological functions within this cellular compartment. Peptide profiling analysis provides evidence of cross-talk between N-terminal acetylation and internal modifications in a NAT substrate-specific manner. In vivo studies indicate that N-terminal acetylation is critical for meiosis, as it regulates the assembly of the synaptonemal complex (SC), a proteinaceous structure ubiquitously present during meiosis from yeast to humans. Specifically, N-terminal acetylation of NatB substrate SYP-1, an SC structural component, is critical for SC assembly. These findings provide novel insights into the biological functions of N-terminal acetylation and its essential role during meiosis.
[Mh] Termos MeSH primário: Caenorhabditis elegans/metabolismo
Acetiltransferase N-Terminal B/metabolismo
Complexo Sinaptonêmico/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Animais
Caenorhabditis elegans/enzimologia
Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/metabolismo
Núcleo Celular/metabolismo
Meiose/genética
Mutação
Acetiltransferase N-Terminal B/genética
Proteínas Nucleares/metabolismo
Proteoma
Complexo Sinaptonêmico/química
Complexo Sinaptonêmico/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Nuclear Proteins); 0 (Proteome); 0 (SYP-1 protein, C elegans); EC 2.3.1.88 (N-Terminal Acetyltransferase B)
[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:161125
[St] Status:MEDLINE


  3 / 24 MEDLINE  
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[PMID]:26600389
[Au] Autor:Yasuda K; Takahashi M; Mori N
[Ad] Endereço:The Department of Anatomy and Neurobiology, Nagasaki University School of Medicine, Nagasaki, Japan.
[Ti] Título:Mdm20 Modulates Actin Remodeling through the mTORC2 Pathway via Its Effect on Rictor Expression.
[So] Source:PLoS One;10(11):e0142943, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:NatB is an N-terminal acetyltransferase consisting of a catalytic Nat5 subunit and an auxiliary Mdm20 subunit. In yeast, NatB acetylates N-terminal methionines of proteins during de novo protein synthesis and also regulates actin remodeling through N-terminal acetylation of tropomyosin (Trpm), which stabilizes the actin cytoskeleton by interacting with actin. However, in mammalian cells, the biological functions of the Mdm20 and Nat5 subunits are not well understood. In the present study, we show for the first time that Mdm20-knockdown (KD), but not Nat5-KD, in HEK293 and HeLa cells suppresses not only cell growth, but also cellular motility. Although stress fibers were formed in Mdm20-KD cells, and not in control or Nat5-KD cells, the localization of Trpm did not coincide with the formation of stress fibers in Mdm20-KD cells. Notably, knockdown of Mdm20 reduced the expression of Rictor, an mTORC2 complex component, through post-translational regulation. Additionally, PKCαS657 phosphorylation, which regulates the organization of the actin cytoskeleton, was also reduced in Mdm20-KD cells. Our data also suggest that FoxO1 phosphorylation is regulated by the Mdm20-mTORC2-Akt pathway in response to serum starvation and insulin stimulation. Taken together, the present findings suggest that Mdm20 acts as a novel regulator of Rictor, thereby controlling mTORC2 activity, and leading to the activation of PKCαS657 and FoxO1.
[Mh] Termos MeSH primário: Actinas/metabolismo
Proteínas de Transporte/metabolismo
Complexos Multiproteicos/metabolismo
Acetiltransferase N-Terminal B/metabolismo
Serina-Treonina Quinases TOR/metabolismo
[Mh] Termos MeSH secundário: Acetiltransferases/deficiência
Acetiltransferases/metabolismo
Citoesqueleto de Actina/metabolismo
Ciclo Celular
Movimento Celular
Proliferação Celular
Ativação Enzimática
Proteína Forkhead Box O1
Fatores de Transcrição Forkhead/metabolismo
Regulação da Expressão Gênica
Células HEK293
Células HeLa
Células Hep G2
Seres Humanos
Alvo Mecanístico do Complexo 2 de Rapamicina
Modelos Biológicos
Acetiltransferase N-Terminal B/deficiência
Fosforilação
Processamento de Proteína Pós-Traducional
Transporte Proteico
Proteínas Proto-Oncogênicas c-akt/metabolismo
Proteína Companheira de mTOR Insensível à Rapamicina
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); 0 (Carrier Proteins); 0 (FOXO1 protein, human); 0 (Forkhead Box Protein O1); 0 (Forkhead Transcription Factors); 0 (Multiprotein Complexes); 0 (RICTOR protein, human); 0 (Rapamycin-Insensitive Companion of mTOR Protein); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (NatB protein, S cerevisiae); EC 2.3.1.88 (N-Terminal Acetyltransferase B); EC 2.3.1.88 (NAA25 protein, human); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 2); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151125
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0142943


  4 / 24 MEDLINE  
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[PMID]:26361095
[Au] Autor:Kapos P; Xu F; Meinnel T; Giglione C; Li X
[Ad] Endereço:a Michael Smith Laboratories; University of British Columbia ; British Columbia , Canada.
[Ti] Título:N-terminal modifications contribute to flowering time and immune response regulations.
[So] Source:Plant Signal Behav;10(10):e1073874, 2015.
[Is] ISSN:1559-2324
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A variety of N-terminal co-translational modifications play crucial roles in many cellular processes across eukaryotic organisms. Recently, N-terminal acetylation has been proposed as a regulatory mechanism for the control of plant immunity. Analysis of an N-terminal acetyltransferase complex A (NatA) mutant, naa15-1, revealed that NatA controls the stability of immune receptor Suppressor of NPR1, Constitutive 1 (SNC1) in an antagonistic fashion with NatB. Here, we further report on an antagonistic regulation of flowering time by NatA and NatB, where naa15-1 plants exhibit late flowering, opposite of the early flowering phenotype previously observed in natB mutants. In addition, we provide evidence for the involvement of another N-terminal modification, N-myristoylation, in controlling pathogen-associated molecular pattern (PAMP) triggered immunity (PTI) through the characterization of N-myristoyltransferase 1 (NMT1) defective mutants, which express a low level of NMT1 protein. The mutant line lacks induced production of reactive oxygen species and MAP kinase phosphorylation in response to treatment with the known immune elicitor flg22. NMT1 deficient plants also exhibit increased susceptibility to Pst hrcC, a non-pathogenic Pseudomonas syringae tomato strain lacking a functional type-III secretion system. The potential for the NatA-NatB antagonistic relationship to exist outside of the regulation of SNC1 as well as the disclosing of NMT1s role in PTI further supports the significant contribution of N-terminal co-translational modifications in the regulation of biological processes in plants, and present interesting areas for further exploration.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/genética
Arabidopsis/genética
Flores/crescimento & desenvolvimento
Regulação da Expressão Gênica de Plantas
Desenvolvimento Vegetal/genética
Imunidade Vegetal/genética
Modificação Traducional de Proteínas
[Mh] Termos MeSH secundário: Acetilação
Aciltransferases/genética
Aciltransferases/metabolismo
Arabidopsis/metabolismo
Arabidopsis/microbiologia
Proteínas de Arabidopsis/metabolismo
Flores/metabolismo
Metiltransferases/genética
Metiltransferases/metabolismo
Mutação
Acetiltransferase N-Terminal A/genética
Acetiltransferase N-Terminal A/metabolismo
Acetiltransferase N-Terminal B/genética
Acetiltransferase N-Terminal B/metabolismo
Padrões Moleculares Associados a Patógenos/metabolismo
Fenótipo
Pseudomonas syringae
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Pathogen-Associated Molecular Pattern Molecules); 0 (SNC1 protein, Arabidopsis); EC 2.1.1.- (Methyltransferases); EC 2.1.1.- (NMT1 protein, Arabidopsis); EC 2.3.- (Acyltransferases); EC 2.3.1.88 (N-Terminal Acetyltransferase A); EC 2.3.1.88 (N-Terminal Acetyltransferase B); EC 2.3.1.97 (glycylpeptide N-tetradecanoyltransferase)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150912
[St] Status:MEDLINE
[do] DOI:10.1080/15592324.2015.1073874


  5 / 24 MEDLINE  
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[PMID]:25163837
[Au] Autor:Lee KE; Ahn JY; Kim JM; Hwang CS
[Ad] Endereço:Department of Life Sciences, Pohang University of Science and Technology, Gyeongbuk, 790-784, Republic of Korea.
[Ti] Título:Synthetic lethal screen of NAA20, a catalytic subunit gene of NatB N-terminal acetylase in Saccharomyces cerevisiae.
[So] Source:J Microbiol;52(10):842-8, 2014 Oct.
[Is] ISSN:1976-3794
[Cp] País de publicação:Korea (South)
[La] Idioma:eng
[Ab] Resumo:The Saccharomyces cerevisiae NatB N-terminal acetylase contains a catalytic subunit Naa20 and an auxiliary subunit Naa25. To elucidate the cellular functions of the NatB, we utilized the Synthetic Genetic Array to screen for genes that are essential for cell growth in the absence of NAA20. The genome-wide synthetic lethal screen of NAA20 identified genes encoding for serine/threonine protein kinase Vps15, 1,3-beta-glucanosyltransferase Gas5, and a catabolic repression regulator Mig3. The present study suggests that the catalytic activity of the NatB N-terminal aceytase is involved in vacuolar protein sorting and cell wall maintenance.
[Mh] Termos MeSH primário: Deleção de Genes
Genes Essenciais
Acetiltransferase N-Terminal B/genética
Acetiltransferase N-Terminal B/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/fisiologia
[Mh] Termos MeSH secundário: Domínio Catalítico/genética
Genes Fúngicos
Glucosiltransferases/genética
Glucosiltransferases/metabolismo
Proteínas Repressoras/genética
Proteínas Repressoras/metabolismo
Saccharomyces cerevisiae/crescimento & desenvolvimento
Proteína VPS15 de Distribuição Vacuolar/genética
Proteína VPS15 de Distribuição Vacuolar/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Mig3 protein, S cerevisiae); 0 (Repressor Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 2.3.1.88 (N-Terminal Acetyltransferase B); EC 2.3.1.88 (Nat3 protein, S cerevisiae); EC 2.4.1.- (GAS5 protein, S cerevisiae); EC 2.4.1.- (Glucosyltransferases); EC 2.7.11.1 (VPS15 protein, S cerevisiae); EC 2.7.11.1 (Vacuolar Sorting Protein VPS15)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140829
[St] Status:MEDLINE
[do] DOI:10.1007/s12275-014-3694-z


  6 / 24 MEDLINE  
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[PMID]:24358196
[Au] Autor:Yasuda K; Ohyama K; Onga K; Kakizuka A; Mori N
[Ad] Endereço:From the Department of Anatomy and Neurobiology, Nagasaki University School of Medicine, Nagasaki, Japan.
[Ti] Título:Mdm20 stimulates polyQ aggregation via inhibiting autophagy through Akt-Ser473 phosphorylation.
[So] Source:PLoS One;8(12):e82523, 2013.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mdm20 is an auxiliary subunit of the NatB complex, which includes Nat5, the catalytic subunit for protein N-terminal acetylation. The NatB complex catalyzes N-acetylation during de novo protein synthesis initiation; however, recent evidence from yeast suggests that NatB also affects post-translational modification of tropomyosin, which is involved in intracellular sorting of aggregated proteins. We hypothesized that an acetylation complex such as NatB may contribute to protein clearance and/or proteostasis in mammalian cells. Using a poly glutamine (polyQ) aggregation system, we examined whether the NatB complex or its components affect protein aggregation in rat primary cultured hippocampal neurons and HEK293 cells. The number of polyQ aggregates increased in Mdm20 over-expressing (OE) cells, but not in Nat5-OE cells. Conversely, in Mdm20 knockdown (KD) cells, but not in Nat5-KD cells, polyQ aggregation was significantly reduced. Although Mdm20 directly associates with Nat5, the overall cellular localization of the two proteins was slightly distinct, and Mdm20 apparently co-localized with the polyQ aggregates. Furthermore, in Mdm20-KD cells, a punctate appearance of LC3 was evident, suggesting the induction of autophagy. Consistent with this notion, phosphorylation of Akt, most notably at Ser473, was greatly reduced in Mdm20-KD cells. These results demonstrate that Mdm20, the so-called auxiliary subunit of the translation-coupled protein N-acetylation complex, contributes to protein clearance and/or aggregate formation by affecting the phosphorylation level of Akt indepenently from the function of Nat5.
[Mh] Termos MeSH primário: Autofagia/fisiologia
Acetiltransferase N-Terminal B/metabolismo
Neurônios/metabolismo
Peptídeos/metabolismo
Proteínas Proto-Oncogênicas c-akt/metabolismo
[Mh] Termos MeSH secundário: Animais
Células HEK293
Hipocampo/metabolismo
Seres Humanos
Fosforilação
Processamento de Proteína Pós-Traducional
Ratos
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Peptides); 26700-71-0 (polyglutamine); EC 2.3.1.88 (N-Terminal Acetyltransferase B); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
[Em] Mês de entrada:1409
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131221
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0082523


  7 / 24 MEDLINE  
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[PMID]:24244708
[Au] Autor:Ferrández-Ayela A; Micol-Ponce R; Sánchez-García AB; Alonso-Peral MM; Micol JL; Ponce MR
[Ad] Endereço:Instituto de Bioingeniería, Universidad Miguel Hernández, Campus de Elche, Elche, Spain.
[Ti] Título:Mutation of an Arabidopsis NatB N-alpha-terminal acetylation complex component causes pleiotropic developmental defects.
[So] Source:PLoS One;8(11):e80697, 2013.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:N-α-terminal acetylation is one of the most common, but least understood modifications of eukaryotic proteins. Although a high degree of conservation exists between the N-α-terminal acetylomes of plants and animals, very little information is available on this modification in plants. In yeast and humans, N-α-acetyltransferase complexes include a single catalytic subunit and one or two auxiliary subunits. Here, we report the positional cloning of TRANSCURVATA2 (TCU2), which encodes the auxiliary subunit of the NatB N-α-acetyltransferase complex in Arabidopsis. The phenotypes of loss-of-function tcu2 alleles indicate that NatB complex activity is required for flowering time regulation and for leaf, inflorescence, flower, fruit and embryonic development. In double mutants, tcu2 alleles synergistically interact with alleles of ARGONAUTE10, which encodes a component of the microRNA machinery. In summary, NatB-mediated N-α-terminal acetylation of proteins is pleiotropically required for Arabidopsis development and seems to be functionally related to the microRNA pathway.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/genética
Proteínas de Arabidopsis/metabolismo
Arabidopsis/genética
Arabidopsis/metabolismo
Acetiltransferase N-Terminal B/genética
Acetiltransferase N-Terminal B/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Arabidopsis/crescimento & desenvolvimento
Proteínas Argonauta/genética
Proteínas Argonauta/metabolismo
MicroRNAs/genética
MicroRNAs/metabolismo
Mutação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AGO10 protein, Arabidopsis); 0 (Arabidopsis Proteins); 0 (Argonaute Proteins); 0 (MicroRNAs); EC 2.3.1.88 (N-Terminal Acetyltransferase B)
[Em] Mês de entrada:1502
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131119
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0080697


  8 / 24 MEDLINE  
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[PMID]:23403232
[Au] Autor:Mathiasen DP; Gallina I; Germann SM; Hamou W; Eléouët M; Thodberg S; Eckert-Boulet N; Game J; Lisby M
[Ad] Endereço:Department of Biology, University of Copenhagen, Ole Maaloeesvej 5, DK-2200 Copenhagen N, Denmark.
[Ti] Título:Physical mapping and cloning of RAD56.
[So] Source:Gene;519(1):182-6, 2013 Apr 25.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Here we report the physical mapping of the rad56-1 mutation to the NAT3 gene, which encodes the catalytic subunit of the NatB N-terminal acetyltransferase in Saccharomyces cerevisiae. Mutation of RAD56 causes sensitivity to X-rays, methyl methanesulfonate, zeocin, camptothecin and hydroxyurea, but not to UV light, suggesting that N-terminal acetylation of specific DNA repair proteins is important for efficient DNA repair.
[Mh] Termos MeSH primário: Mapeamento Cromossômico
Clonagem Molecular
Mutação
Acetiltransferase N-Terminal B/genética
Proteínas de Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Acetilação
Bleomicina/efeitos adversos
Camptotecina/efeitos adversos
Dano ao DNA
Reparo do DNA
DNA Fúngico/genética
Hidroxiureia/efeitos adversos
Metanossulfonato de Metila/efeitos adversos
Acetiltransferase N-Terminal B/metabolismo
Fenótipo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Análise de Sequência de DNA
Raios X/efeitos adversos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Fungal); 0 (Saccharomyces cerevisiae Proteins); 11056-06-7 (Bleomycin); 181494-14-4 (Zeocin); AT5C31J09G (Methyl Methanesulfonate); EC 2.3.1.88 (N-Terminal Acetyltransferase B); EC 2.3.1.88 (Nat3 protein, S cerevisiae); X6Q56QN5QC (Hydroxyurea); XT3Z54Z28A (Camptothecin)
[Em] Mês de entrada:1305
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130214
[St] Status:MEDLINE


  9 / 24 MEDLINE  
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[PMID]:23363603
[Au] Autor:Zattas D; Adle DJ; Rubenstein EM; Hochstrasser M
[Ad] Endereço:Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.
[Ti] Título:N-terminal acetylation of the yeast Derlin Der1 is essential for Hrd1 ubiquitin-ligase activity toward luminal ER substrates.
[So] Source:Mol Biol Cell;24(7):890-900, 2013 Apr.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Two conserved ubiquitin ligases, Hrd1 and Doa10, mediate most endoplasmic reticulum-associated protein degradation (ERAD) in yeast. Degradation signals (degrons) recognized by these ubiquitin ligases remain poorly characterized. Doa10 recognizes the Deg1 degron from the MATα2 transcription factor. We previously found that deletion of the gene (NAT3) encoding the catalytic subunit of the NatB N-terminal acetyltransferase weakly stabilized a Deg1-fusion protein. By contrast, a recent analysis of several MATα2 derivatives suggested that N-terminal acetylation of these proteins by NatB was crucial for recognition by Doa10. We now analyze endogenous MATα2 degradation in cells lacking NatB and observe minimal perturbation relative to wild-type cells. However, NatB mutation strongly impairs degradation of ER-luminal Hrd1 substrates. This unexpected defect derives from a failure of Der1, a Hrd1 complex subunit, to be N-terminally acetylated in NatB mutant yeast. We retargeted Der1 to another acetyltransferase to show that it is the only ERAD factor requiring N-terminal acetylation. Preventing Der1 acetylation stimulates its proteolysis via the Hrd1 pathway, at least partially accounting for the ERAD defect observed in the absence of NatB. These results reveal an important role for N-terminal acetylation in controlling Hrd1 ligase activity toward a specific class of ERAD substrates.
[Mh] Termos MeSH primário: Degradação Associada com o Retículo Endoplasmático
Proteínas de Membrana/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Acetiltransferases/genética
Acetiltransferases/metabolismo
Sequência de Aminoácidos
Retículo Endoplasmático/metabolismo
Immunoblotting
Transferases Intramoleculares/genética
Transferases Intramoleculares/metabolismo
Espectrometria de Massas
Proteínas de Membrana/química
Proteínas de Membrana/genética
Dados de Sequência Molecular
Mutação
Acetiltransferase N-Terminal B/genética
Acetiltransferase N-Terminal B/metabolismo
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Transdução de Sinais/genética
Ubiquitina-Proteína Ligases/genética
Resposta a Proteínas não Dobradas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (DER1 protein, S cerevisiae); 0 (MATA2 protein, S cerevisiae); 0 (Membrane Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (NatB protein, S cerevisiae); EC 2.3.1.88 (N-Terminal Acetyltransferase B); EC 2.3.1.88 (Nat3 protein, S cerevisiae); EC 2.3.2.27 (HRD1 protein, S cerevisiae); EC 2.3.2.27 (SSM4 protein, S cerevisiae); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 5.4.- (Intramolecular Transferases); EC 5.4.99.- (DEG1 protein, S cerevisiae)
[Em] Mês de entrada:1309
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130201
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E12-11-0838


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[PMID]:22326526
[Au] Autor:Kisand K; Uibo R
[Ad] Endereço:University of Tartu, Estonia. kalle.kisand@ut.ee
[Ti] Título:LADA and T1D in Estonian population - two different genetic risk profiles.
[So] Source:Gene;497(2):285-91, 2012 Apr 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:AIMS/HYPOTHESIS: The aim of our study was to analyze combined impact of 17 polymorphisms at 8 gene regions previously shown to be associated with autoimmunity in diabetes. We hypothesized that the genetic predisposition is multiplicative and joint risk of different diabetic phenotypes forms by distinct combination of susceptibility loci. METHODS: An ethnically homogenous population of Estonian origin, including 65 LADA patients, 154 patients with T1D, 260 patients with T2D and 229 non-diabetic controls, was genotyped for polymorphisms/haplotypes in HLA-DQB1, insulin gene (rs689, rs3842729), PHTF1-PTPN22 region (rs2476601, rs6679677), CTLA4 region (rs231806, rs16840252, rs5742909, rs231775, rs3087243, rs2033171), ICOS region (rs10932037, rs4675379), CD25 (rs706778), CD226(rs763361), NAA25 (rs17696736). RESULTS: As expected, the risk of T1D was consistently attributed by HLA-DQB1 haplotypes, but also by haplotypes of INS and PHTF1-PTPN22 region, and rs17696736 in NAA25. By contrast, LADA was associated only with T1D-protective HLA haplotypes and with two more frequent haplotypes of the CTLA4. It is of interest, that seldom CT haplotype of PHTF1-PTPN22 region carried the risk for autoantibody-negative T2D. The final best-fitted model for T1D genetic risk contained six gene regions (HLA-DQB1, INS, PHTF1, CTLA4 +49, CD226 and NAA25) and for LADA only two (HLA-DQB1 and CTLA4 +49). The AUCs of these models are 0.869 and 0.693, respectively. CONCLUSIONS: Classical T1D-risk haplotypes of HLA and some non-HLA loci describe quite well the genetic risk for T1D but not for LADA. The need of further studies should be stressed to discover the real risk factors for slower forms of autoimmune diabetes in adults.
[Mh] Termos MeSH primário: Diabetes Mellitus Tipo 1/genética
Diabetes Mellitus Tipo 1/imunologia
Predisposição Genética para Doença/genética
[Mh] Termos MeSH secundário: Acetiltransferases/genética
Acetiltransferases/imunologia
Adulto
Idade de Início
Alelos
Antígenos de Diferenciação de Linfócitos T/genética
Antígeno CTLA-4/genética
Antígeno CTLA-4/imunologia
Diabetes Mellitus Tipo 1/epidemiologia
Diabetes Mellitus Tipo 2/genética
Diabetes Mellitus Tipo 2/imunologia
Estônia/epidemiologia
Grupo com Ancestrais do Continente Europeu
Evolução Molecular
Feminino
Loci Gênicos/genética
Loci Gênicos/imunologia
Predisposição Genética para Doença/epidemiologia
Genética Populacional/métodos
Cadeias beta de HLA-DQ/genética
Cadeias beta de HLA-DQ/imunologia
Haplótipos
Proteínas de Homeodomínio/genética
Proteínas de Homeodomínio/imunologia
Seres Humanos
Proteína Coestimuladora de Linfócitos T Induzíveis/genética
Proteína Coestimuladora de Linfócitos T Induzíveis/imunologia
Insulina/genética
Insulina/imunologia
Subunidade alfa de Receptor de Interleucina-2/genética
Subunidade alfa de Receptor de Interleucina-2/imunologia
Masculino
Meia-Idade
Acetiltransferase N-Terminal B
Fenótipo
Polimorfismo Genético
Proteína Tirosina Fosfatase não Receptora Tipo 22/genética
Proteína Tirosina Fosfatase não Receptora Tipo 22/imunologia
Risco
Fatores de Transcrição/genética
Fatores de Transcrição/imunologia
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, Differentiation, T-Lymphocyte); 0 (CD226 antigen); 0 (CTLA-4 Antigen); 0 (CTLA4 protein, human); 0 (HLA-DQ beta-Chains); 0 (HLA-DQB1 antigen); 0 (Homeodomain Proteins); 0 (ICOS protein, human); 0 (IL2RA protein, human); 0 (Inducible T-Cell Co-Stimulator Protein); 0 (Insulin); 0 (Interleukin-2 Receptor alpha Subunit); 0 (PHTF1 protein, human); 0 (Transcription Factors); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.88 (N-Terminal Acetyltransferase B); EC 2.3.1.88 (NAA25 protein, human); EC 3.1.3.48 (PTPN22 protein, human); EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 22)
[Em] Mês de entrada:1207
[Cu] Atualização por classe:121115
[Lr] Data última revisão:
121115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120214
[St] Status:MEDLINE
[do] DOI:10.1016/j.gene.2012.01.089



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