Base de dados : MEDLINE
Pesquisa : D08.811.913.050.134.423.600 [Categoria DeCS]
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[PMID]:28196861
[Au] Autor:Aksnes H; Goris M; Strømland Ø; Drazic A; Waheed Q; Reuter N; Arnesen T
[Ad] Endereço:From the Department of Molecular Biology, University of Bergen, N-5020 Bergen.
[Ti] Título:Molecular determinants of the N-terminal acetyltransferase Naa60 anchoring to the Golgi membrane.
[So] Source:J Biol Chem;292(16):6821-6837, 2017 Apr 21.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:α-Acetyltransferase 60 (Naa60 or NatF) was recently identified as an unconventional N-terminal acetyltransferase (NAT) because it localizes to organelles, in particular the Golgi apparatus, and has a preference for acetylating N termini of the transmembrane proteins. This knowledge challenged the prevailing view of N-terminal acetylation as a co-translational ribosome-associated process and suggested a new mechanistic functioning for the enzymes responsible for this increasingly recognized protein modification. Crystallography studies on Naa60 were unable to resolve the C-terminal tail of Naa60, which is responsible for the organellar localization. Here, we combined modeling, assays, and cellular localization studies to investigate the secondary structure and membrane interacting capacity of Naa60. The results show that Naa60 is a peripheral membrane protein. Two amphipathic helices within the Naa60 C terminus bind the membrane directly in a parallel position relative to the lipid bilayer via hydrophobic and electrostatic interactions. A peptide corresponding to the C terminus was unstructured in solution and only folded into an α-helical conformation in the presence of liposomes. Computational modeling and cellular mutational analysis revealed the hydrophobic face of two α-helices to be critical for membranous localization. Furthermore, we found a strong and specific binding preference of Naa60 toward membranes containing the phosphatidylinositol PI(4)P, thus possibly explaining the primary residency of Naa60 at the PI(4)P-rich Golgi. In conclusion, we have defined the mode of cytosolic Naa60 anchoring to the Golgi apparatus, most likely occurring post-translationally and specifically facilitating post-translational N-terminal acetylation of many transmembrane proteins.
[Mh] Termos MeSH primário: Complexo de Golgi/metabolismo
Acetiltransferase N-Terminal F/química
[Mh] Termos MeSH secundário: Calorimetria
Dicroísmo Circular
Cristalografia por Raios X
Citosol/enzimologia
Análise Mutacional de DNA
Proteínas de Fluorescência Verde/química
Células HeLa
Seres Humanos
Ligações de Hidrogênio
Bicamadas Lipídicas/química
Lipossomos/química
Simulação de Dinâmica Molecular
Mutagênese Sítio-Dirigida
Peptídeos/química
Ligação Proteica
Domínios Proteicos
Estrutura Secundária de Proteína
Ribossomos/química
Eletricidade Estática
Triptofano/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lipid Bilayers); 0 (Liposomes); 0 (Peptides); 147336-22-9 (Green Fluorescent Proteins); 8DUH1N11BX (Tryptophan); EC 2.3.1.88 (N-Terminal Acetyltransferase F); EC 2.3.1.88 (NAA60 protein, human)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170621
[Lr] Data última revisão:
170621
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170216
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.770362


  2 / 5 MEDLINE  
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[PMID]:27320834
[Au] Autor:Støve SI; Magin RS; Foyn H; Haug BE; Marmorstein R; Arnesen T
[Ad] Endereço:Department of Molecular Biology, University of Bergen, 5020 Bergen, Norway; Department of Surgery, Haukeland University Hospital, 5021 Bergen, Norway.
[Ti] Título:Crystal Structure of the Golgi-Associated Human Nα-Acetyltransferase 60 Reveals the Molecular Determinants for Substrate-Specific Acetylation.
[So] Source:Structure;24(7):1044-56, 2016 Jul 06.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:N-Terminal acetylation is a common and important protein modification catalyzed by N-terminal acetyltransferases (NATs). Six human NATs (NatA-NatF) contain one catalytic subunit each, Naa10 to Naa60, respectively. In contrast to the ribosome-associated NatA to NatE, NatF/Naa60 specifically associates with Golgi membranes and acetylates transmembrane proteins. To gain insight into the molecular basis for the function of Naa60, we developed an Naa60 bisubstrate CoA-peptide conjugate inhibitor, determined its X-ray structure when bound to CoA and inhibitor, and carried out biochemical experiments. We show that Naa60 adapts an overall fold similar to that of the catalytic subunits of ribosome-associated NATs, but with the addition of two novel elongated loops that play important roles in substrate-specific binding. One of these loops mediates a dimer to monomer transition upon substrate-specific binding. Naa60 employs a catalytic mechanism most similar to Naa50. Collectively, these data reveal the molecular basis for Naa60-specific acetyltransferase activity with implications for its Golgi-specific functions.
[Mh] Termos MeSH primário: Acetiltransferase N-Terminal F/química
[Mh] Termos MeSH secundário: Domínio Catalítico
Cristalografia por Raios X
Estabilidade Enzimática
Complexo de Golgi/metabolismo
Seres Humanos
Membranas Intracelulares/metabolismo
Acetiltransferase N-Terminal F/metabolismo
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.3.1.88 (N-Terminal Acetyltransferase F); EC 2.3.1.88 (NAA60 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160621
[St] Status:MEDLINE


  3 / 5 MEDLINE  
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[PMID]:26164078
[Au] Autor:Aksnes H; Marie M; Arnesen T
[Ad] Endereço:Department of Molecular Biology, University of Bergen, Bergen, Norway.
[Ti] Título:Holding it together: Naa60 at the Golgi.
[So] Source:Oncotarget;6(18):15726-7, 2015 Jun 30.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Complexo de Golgi/enzimologia
Acetiltransferase N-Terminal F/metabolismo
[Mh] Termos MeSH secundário: Seres Humanos
[Pt] Tipo de publicação:EDITORIAL
[Nm] Nome de substância:
EC 2.3.1.88 (N-Terminal Acetyltransferase F); EC 2.3.1.88 (NAA60 protein, human)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:151027
[Lr] Data última revisão:
151027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150713
[St] Status:MEDLINE


  4 / 5 MEDLINE  
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[PMID]:25732826
[Au] Autor:Aksnes H; Van Damme P; Goris M; Starheim KK; Marie M; Støve SI; Hoel C; Kalvik TV; Hole K; Glomnes N; Furnes C; Ljostveit S; Ziegler M; Niere M; Gevaert K; Arnesen T
[Ad] Endereço:Department of Molecular Biology, University of Bergen, 5020 Bergen, Norway.
[Ti] Título:An organellar nα-acetyltransferase, naa60, acetylates cytosolic N termini of transmembrane proteins and maintains Golgi integrity.
[So] Source:Cell Rep;10(8):1362-74, 2015 Mar 03.
[Is] ISSN:2211-1247
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:N-terminal acetylation is a major and vital protein modification catalyzed by N-terminal acetyltransferases (NATs). NatF, or Nα-acetyltransferase 60 (Naa60), was recently identified as a NAT in multicellular eukaryotes. Here, we find that Naa60 differs from all other known NATs by its Golgi localization. A new membrane topology assay named PROMPT and a selective membrane permeabilization assay established that Naa60 faces the cytosolic side of intracellular membranes. An Nt-acetylome analysis of NAA60-knockdown cells revealed that Naa60, as opposed to other NATs, specifically acetylates transmembrane proteins and has a preference for N termini facing the cytosol. Moreover, NAA60 knockdown causes Golgi fragmentation, indicating an important role in the maintenance of the Golgi's structural integrity. This work identifies a NAT associated with membranous compartments and establishes N-terminal acetylation as a common modification among transmembrane proteins, a thus-far poorly characterized part of the N-terminal acetylome.
[Mh] Termos MeSH primário: Complexo de Golgi/metabolismo
Proteínas de Membrana/metabolismo
Acetiltransferase N-Terminal F/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Sequência de Aminoácidos
Membrana Celular/metabolismo
Citosol/metabolismo
Complexo de Golgi/patologia
Células HEK293
Células HeLa
Seres Humanos
Acetiltransferase N-Terminal F/antagonistas & inibidores
Acetiltransferase N-Terminal F/genética
Processamento de Proteína Pós-Traducional
Estrutura Terciária de Proteína
Interferência de RNA
RNA Interferente Pequeno/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (RNA, Small Interfering); EC 2.3.1.88 (N-Terminal Acetyltransferase F); EC 2.3.1.88 (NAA60 protein, human)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:150305
[Lr] Data última revisão:
150305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150304
[St] Status:MEDLINE


  5 / 5 MEDLINE  
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[PMID]:23942880
[Au] Autor:Wang Y; Black BA; Curtis JM; Gänzle MG
[Ad] Endereço:Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, AB, Canada.
[Ti] Título:Characterization of α-galacto-oligosaccharides formed via heterologous expression of α-galactosidases from Lactobacillus reuteri in Lactococcus lactis.
[So] Source:Appl Microbiol Biotechnol;98(6):2507-17, 2014 Mar.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:α-Galacto-oligosaccharides (α-GOS) are produced by transgalactosylation reactions of α-galactosidase (α-Gal) or by conversion of raffinose family oligosaccharides by levansucrase. Similarly to ß-GOS, α-GOS have the potential to mimic glycan receptors on eukaryotic cells and act as molecular decoys to prevent bacterial infection; however, data on transgalactosylation reactions of α-Gal remain scarce. The α-Gal gene sequence from Lactobacillus reuteri was cloned into an α-Gal negative strain of Lactococcus lactis. Transgalactosylation reactions were achieved using crude cell extracts with melibiose or raffinose as galactosyl donor and fucose, N-acetylglucosamine or lactose as galactosyl acceptor. The composition, sequence and most linkage types of α-GOS formed with acceptors saccharides were determined by liquid chromatography-tandem mass spectrometry. α-Gal of Lactobacillus reuteri formed (1 → 3)-, (1 → 4)- or (1 → 6)-linked α-GOS but exhibited a preference for formation of (1 → 6)-linkages. Fucose, N-acetylglucosamine and lactose were suitable galactosyl acceptors for α-Gal of L. reuteri, resulting in formation of (1 → 3)-, (1 → 4)- or (1 → 6)-linked hetero-oligosaccharides. By determining the structural specificity of α-Gal and increasing the variation of oligosaccharides produced by introducing alternative acceptor sugars, this work supports further studies to assess α-GOS pathogen adhesion prevention in mammalian hosts.
[Mh] Termos MeSH primário: Lactobacillus reuteri/enzimologia
Lactococcus lactis/enzimologia
Oligossacarídeos/química
Oligossacarídeos/metabolismo
alfa-Galactosidase/genética
alfa-Galactosidase/metabolismo
[Mh] Termos MeSH secundário: Acetilglucosamina/metabolismo
Cromatografia Líquida
Clonagem Molecular
Fucose/metabolismo
Expressão Gênica
Glicosilação
Lactobacillus reuteri/genética
Lactococcus lactis/genética
Lactose/metabolismo
Melibiose/metabolismo
Acetiltransferase N-Terminal F
Rafinose/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Oligosaccharides); 0 (Recombinant Proteins); 28RYY2IV3F (Fucose); 9B1VBE526I (Melibiose); EC 2.3.1.88 (N-Terminal Acetyltransferase F); EC 3.2.1.22 (alpha-Galactosidase); J2B2A4N98G (Lactose); N5O3QU595M (Raffinose); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130815
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-013-5145-x



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