Base de dados : MEDLINE
Pesquisa : D12.776.580.612 [Categoria DeCS]
Referências encontradas : 203 [refinar]
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[PMID]:28615450
[Au] Autor:Upadhyay AS; Stehling O; Panayiotou C; Rösser R; Lill R; Överby AK
[Ad] Endereço:From the Department of Clinical Microbiology, Virology, Umeå University, 90185 Umeå, Sweden.
[Ti] Título:Cellular requirements for iron-sulfur cluster insertion into the antiviral radical SAM protein viperin.
[So] Source:J Biol Chem;292(33):13879-13889, 2017 Aug 18.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Viperin (RSAD2) is an interferon-stimulated antiviral protein that belongs to the radical -adenosylmethionine (SAM) enzyme family. Viperin's iron-sulfur (Fe/S) cluster is critical for its antiviral activity against many different viruses. CIA1 (CIAO1), an essential component of the cytosolic iron-sulfur protein assembly (CIA) machinery, is crucial for Fe/S cluster insertion into viperin and hence for viperin's antiviral activity. In the CIA pathway, CIA1 cooperates with CIA2A, CIA2B, and MMS19 targeting factors to form various complexes that mediate the dedicated maturation of specific Fe/S recipient proteins. To date, however, the mechanisms of how viperin acquires its radical SAM Fe/S cluster to gain antiviral activity are poorly understood. Using co-immunoprecipitation and Fe-radiolabeling experiments, we therefore studied the roles of CIA2A, CIA2B, and MMS19 for Fe/S cluster insertion. CIA2B and MMS19 physically interacted with the C terminus of viperin and used CIA1 as the primary viperin-interacting protein. In contrast, CIA2A bound to viperin's N terminus in a CIA1-, CIA2B-, and MMS19-independent fashion. Of note, the observed interaction of both CIA2 isoforms with a single Fe/S target protein is unprecedented in the CIA pathway. Fe-radiolabeling experiments with human cells depleted of CIA1, CIA2A, CIA2B, or MMS19 revealed that CIA1, but none of the other CIA factors, is predominantly required for Fe/S cluster incorporation into viperin. Collectively, viperin maturation represents a novel CIA pathway with a minimal requirement of the CIA-targeting factors and represents a new paradigm for the insertion of the Fe/S cofactor into a radical SAM protein.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Proteínas com Ferro-Enxofre/metabolismo
Metalochaperonas/metabolismo
Modelos Biológicos
Proteínas Nucleares/metabolismo
Proteínas/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Apoproteínas/química
Apoproteínas/genética
Apoproteínas/metabolismo
Proteínas de Transporte/antagonistas & inibidores
Proteínas de Transporte/química
Proteínas de Transporte/genética
Células HEK293
Seres Humanos
Imunoprecipitação
Ferro/química
Ferro/metabolismo
Radioisótopos de Ferro
Proteínas com Ferro-Enxofre/química
Proteínas com Ferro-Enxofre/genética
Metalochaperonas/antagonistas & inibidores
Metalochaperonas/química
Metalochaperonas/genética
Mutação
Proteínas Nucleares/antagonistas & inibidores
Proteínas Nucleares/química
Proteínas Nucleares/genética
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Domínios e Motivos de Interação entre Proteínas
Proteínas/química
Proteínas/genética
Interferência de RNA
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Fatores de Transcrição/antagonistas & inibidores
Fatores de Transcrição/química
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apoproteins); 0 (CIAO1 protein, human); 0 (Carrier Proteins); 0 (FAM96B protein, human); 0 (Fam96a protein, human); 0 (Iron Radioisotopes); 0 (Iron-Sulfur Proteins); 0 (MMS19 protein, human); 0 (Metallochaperones); 0 (Nuclear Proteins); 0 (Peptide Fragments); 0 (Proteins); 0 (RSAD2 protein, human); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (Transcription Factors); E1UOL152H7 (Iron)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.780122


  2 / 203 MEDLINE  
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[PMID]:28549213
[Au] Autor:Dolgova NV; Yu C; Cvitkovic JP; Hodak M; Nienaber KH; Summers KL; Cotelesage JJH; Bernholc J; Kaminski GA; Pickering IJ; George GN; Dmitriev OY
[Ad] Endereço:Department of Biochemistry, University of Saskatchewan , Saskatoon, Saskatchewan, Canada , S7N 5E5.
[Ti] Título:Binding of Copper and Cisplatin to Atox1 Is Mediated by Glutathione through the Formation of Metal-Sulfur Clusters.
[So] Source:Biochemistry;56(24):3129-3141, 2017 Jun 20.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Copper is an essential nutrient required for many biological processes involved in primary metabolism, but free copper is toxic due to its ability to catalyze formation of free radicals. To prevent toxic effects, in the cell copper is bound to proteins and low molecular weight compounds, such as glutathione, at all times. The widely used chemotherapy agent cisplatin is known to bind to copper-transporting proteins, including copper chaperone Atox1. Cisplatin interactions with Atox1 and other copper transporters are linked to cancer resistance to platinum-based chemotherapy. Here we analyze the binding of copper and cisplatin to Atox1 in the presence of glutathione under redox conditions that mimic intracellular environment. We show that copper(I) and glutathione form large polymers with a molecular mass of approximately 8 kDa, which can transfer copper to Atox1. Cisplatin also can form polymers with glutathione, albeit at a slower rate. Analysis of simultaneous binding of copper and cisplatin to Atox1 under physiological conditions shows that both metals are bound to the protein through copper-sulfur-platinum bridges.
[Mh] Termos MeSH primário: Cisplatino/metabolismo
Cobre/metabolismo
Glutationa/metabolismo
Metalochaperonas/metabolismo
Platina/metabolismo
Enxofre/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Cisplatino/química
Cobre/química
Glutationa/química
Metalochaperonas/química
Metalochaperonas/isolamento & purificação
Conformação Molecular
Simulação de Dinâmica Molecular
Método de Monte Carlo
Oxirredução
Platina/química
Enxofre/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ATOX1 protein, human); 0 (Metallochaperones); 49DFR088MY (Platinum); 70FD1KFU70 (Sulfur); 789U1901C5 (Copper); GAN16C9B8O (Glutathione); Q20Q21Q62J (Cisplatin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00293


  3 / 203 MEDLINE  
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[PMID]:28543811
[Au] Autor:Levy AR; Turgeman M; Gevorkyan-Aiapetov L; Ruthstein S
[Ad] Endereço:The Department of Chemistry, Faculty of Exact Science, Bar Ilan University, Ramat-Gan, 5290002, Israel.
[Ti] Título:The structural flexibility of the human copper chaperone Atox1: Insights from combined pulsed EPR studies and computations.
[So] Source:Protein Sci;26(8):1609-1618, 2017 Aug.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Metallochaperones are responsible for shuttling metal ions to target proteins. Thus, a metallochaperone's structure must be sufficiently flexible both to hold onto its ion while traversing the cytoplasm and to transfer the ion to or from a partner protein. Here, we sought to shed light on the structure of Atox1, a metallochaperone involved in the human copper regulation system. Atox1 shuttles copper ions from the main copper transporter, Ctr1, to the ATP7b transporter in the Golgi apparatus. Conventional biophysical tools such as X-ray or NMR cannot always target the various conformational states of metallochaperones, owing to a requirement for crystallography or low sensitivity and resolution. Electron paramagnetic resonance (EPR) spectroscopy has recently emerged as a powerful tool for resolving biological reactions and mechanisms in solution. When coupled with computational methods, EPR with site-directed spin labeling and nanoscale distance measurements can provide structural information on a protein or protein complex in solution. We use these methods to show that Atox1 can accommodate at least four different conformations in the apo state (unbound to copper), and two different conformations in the holo state (bound to copper). We also demonstrate that the structure of Atox1 in the holo form is more compact than in the apo form. Our data provide insight regarding the structural mechanisms through which Atox1 can fulfill its dual role of copper binding and transfer.
[Mh] Termos MeSH primário: Apoproteínas/química
Proteínas de Transporte/química
Cobre/química
Metalochaperonas/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Apoproteínas/genética
Apoproteínas/metabolismo
Sítios de Ligação
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Cátions Monovalentes
Dicroísmo Circular
Clonagem Molecular
Cobre/metabolismo
Espectroscopia de Ressonância de Spin Eletrônica
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Seres Humanos
Transporte de Íons
Metalochaperonas/genética
Metalochaperonas/metabolismo
Modelos Moleculares
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ATOX1 protein, human); 0 (Apoproteins); 0 (Carrier Proteins); 0 (Cations, Monovalent); 0 (Metallochaperones); 0 (Recombinant Proteins); 789U1901C5 (Copper)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170824
[Lr] Data última revisão:
170824
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3197


  4 / 203 MEDLINE  
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[PMID]:28425924
[Au] Autor:Blockhuys S; Wittung-Stafshede P
[Ad] Endereço:Department Biology and Biological Engineering, Chalmers University of Technology, 412 96 Gothenburg, Sweden. steblo@chalmers.se.
[Ti] Título:Roles of Copper-Binding Proteins in Breast Cancer.
[So] Source:Int J Mol Sci;18(4), 2017 Apr 20.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Copper ions are needed in several steps of cancer progression. However, the underlying mechanisms, and involved copper-binding proteins, are mainly elusive. Since most copper ions in the body (in and outside cells) are protein-bound, it is important to investigate what copper-binding proteins participate and, for these, how they are loaded with copper by copper transport proteins. Mechanistic information for how some copper-binding proteins, such as extracellular lysyl oxidase (LOX), play roles in cancer have been elucidated but there is still much to learn from a biophysical molecular viewpoint. Here we provide a summary of copper-binding proteins and discuss ones reported to have roles in cancer. We specifically focus on how copper-binding proteins such as mediator of cell motility 1 (MEMO1), LOX, LOX-like proteins, and secreted protein acidic and rich in cysteine (SPARC) modulate breast cancer from molecular and clinical aspects. Because of the importance of copper for invasion/migration processes, which are key components of cancer metastasis, further insights into the actions of copper-binding proteins may provide new targets to combat cancer.
[Mh] Termos MeSH primário: Neoplasias da Mama/metabolismo
Proteínas de Transporte/metabolismo
Cobre/metabolismo
[Mh] Termos MeSH secundário: Animais
Transporte Biológico
Neoplasias da Mama/genética
Neoplasias da Mama/patologia
Proteínas de Transporte/genética
Proliferação Celular
Transformação Celular Neoplásica/genética
Transformação Celular Neoplásica/metabolismo
Feminino
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Metalochaperonas/metabolismo
Modelos Biológicos
Metástase Neoplásica
Neovascularização Patológica/genética
Neovascularização Patológica/metabolismo
Osteonectina/metabolismo
Oxirredução
Proteína-Lisina 6-Oxidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (ATOX1 protein, human); 0 (Carrier Proteins); 0 (Metallochaperones); 0 (Osteonectin); 0 (copper-binding protein); 789U1901C5 (Copper); EC 1.4.3.13 (Protein-Lysine 6-Oxidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170421
[St] Status:MEDLINE


  5 / 203 MEDLINE  
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[PMID]:28320780
[Au] Autor:Yu X; Blanden A; Tsang AT; Zaman S; Liu Y; Gilleran J; Bencivenga AF; Kimball SD; Loh SN; Carpizo DR
[Ad] Endereço:Rutgers Cancer Institute of New Jersey (X.Y., A.T.T., S.Z., Y.L., D.R.C.), Department of Surgery, Rutgers Robert Wood Johnson Medical School (X.Y., A.T.T, Y.L., D.R.C.), Rutgers Translational Sciences, Department of Chemistry and Chemical Biology (S.D.K.), Department of Medicinal Chemistry, Rutgers
[Ti] Título:Thiosemicarbazones Functioning as Zinc Metallochaperones to Reactivate Mutant p53.
[So] Source:Mol Pharmacol;91(6):567-575, 2017 Jun.
[Is] ISSN:1521-0111
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Small-molecule restoration of wild-type structure and function to mutant p53 (so-called mutant reactivation) is a highly sought-after goal in cancer drug development. We previously discovered that small-molecule zinc chelators called (ZMCs) reactivate mutant p53 by restoring zinc binding to zinc-deficient p53 mutants. The lead compound identified from the NCI-60 human tumor cell lines screen, NSC319726 (ZMC1), belongs to the thiosemicarbazone (TSC) class of metal ion chelators that bind iron, copper, magnesium, zinc, and other transition metals. Here, we have investigated the other TSCs, NSC319725 and NSC328784, identified in the same screen, as well as the more well studied TSC, 3-AP (Triapine), to determine whether they function as ZMCs. We measured the zinc zinc ionophore activity, ability to restore zinc to purified p53 DNA binding domain (DBD), and ability to restore site-specific DNA binding to purified R175H-DBD in vitro. We tested all four TSCs in a number of cell-based assays to examine mutant p53 reactivation and the generation of reactive oxygen species (ROS). We found that NSC319725 and NSC328784 behave similarly to ZMC1 in both biophysical and cell-based assays and are heretofore named ZMC2 (NSC319725) and ZMC3 (NSC328784). 3-AP generates a ROS signal similar to ZMC1-3, but it fails to function as a ZMC both in vitro and in cells and ultimately does not reactivate p53. These findings indicate that not all TSCs function as ZMCs, and much of their activity can be predicted by their affinity for zinc.
[Mh] Termos MeSH primário: Inibidores do Crescimento/metabolismo
Metalochaperonas/metabolismo
Mutação/fisiologia
Tiossemicarbazonas/metabolismo
Proteína Supressora de Tumor p53/metabolismo
Zinco/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Proliferação Celular/fisiologia
Relação Dose-Resposta a Droga
Inibidores do Crescimento/farmacologia
Seres Humanos
Mutação/efeitos dos fármacos
Proteína Supressora de Tumor p53/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Growth Inhibitors); 0 (Metallochaperones); 0 (Thiosemicarbazones); 0 (Tumor Suppressor Protein p53); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170614
[Lr] Data última revisão:
170614
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.1124/mol.116.107409


  6 / 203 MEDLINE  
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[PMID]:28294521
[Au] Autor:Hatori Y; Inouye S; Akagi R
[Ad] Endereço:Department of Pharmacy, Yasuda Women's University, Yasuhigashi, Asaminami-ku, Hiroshima, Japan.
[Ti] Título:Thiol-based copper handling by the copper chaperone Atox1.
[So] Source:IUBMB Life;69(4):246-254, 2017 Apr.
[Is] ISSN:1521-6551
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Human antioxidant protein 1 (Atox1) plays a crucial role in cellular copper homeostasis. Atox1 captures cytosolic copper for subsequent transfer to copper pumps in trans Golgi network, thereby facilitating copper supply to various copper-dependent oxidereductases matured within the secretory vesicles. Atox1 and other copper chaperones handle cytosolic copper using Cys thiols which are ideal ligands for coordinating Cu(I). Recent studies demonstrated reversible oxidation of these Cys residues in copper chaperones, linking cellular redox state to copper homeostasis. Highlighted in this review are unique redox properties of Atox1 and other copper chaperones. Also, summarized are the redox nodes in the cytosol which potentially play dominant roles in the redox regulation of copper chaperones. © 2016 IUBMB Life, 69(4):246-254, 2017.
[Mh] Termos MeSH primário: Proteínas de Transporte de Cátions/metabolismo
Cobre/metabolismo
Metalochaperonas/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Transporte de Cátions/genética
Citosol/metabolismo
Seres Humanos
Metalochaperonas/genética
Chaperonas Moleculares/metabolismo
Compostos de Sulfidrila/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (ATOX1 protein, human); 0 (Cation Transport Proteins); 0 (Metallochaperones); 0 (Molecular Chaperones); 0 (Sulfhydryl Compounds); 789U1901C5 (Copper)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE
[do] DOI:10.1002/iub.1620


  7 / 203 MEDLINE  
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[PMID]:28167404
[Au] Autor:Okada M; Miura T; Nakabayashi T
[Ad] Endereço:Graduate School of Pharmaceutical Sciences, Tohoku University, Aoba-ku, Sendai 980-8578, Japan.
[Ti] Título:Comparison of extracellular Cys/Trp motif between Schizosaccharomyces pombe Ctr4 and Ctr5.
[So] Source:J Inorg Biochem;169:97-105, 2017 Apr.
[Is] ISSN:1873-3344
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The reduction and binding of copper ions to the Cys/Trp motif, which is characterized by two cysteines and two tryptophans, in the extracellular N-terminal domain of the copper transporter (Ctr) protein of fungi are investigated using the model peptides of Ctr4 and Ctr5 from Schizosaccharomyces pombe. The Cys/Trp motif of Ctr5 can reduce Cu(II) and ligate Cu(I), which is the same as that of Ctr4 previously reported. Titration of Cu(II) and Cu(I) ions indicates that both the Cys/Trp motifs of Ctr4 and Ctr5 reduce two Cu(II) and bind two Cu(I) per one peptide. However, the coordination structure of the Cu(I)-peptide complex differs between Ctr4 and Ctr5. Cu(I) is bound to the Cys/Trp motif of Ctr5 via cysteine thiolate-Cu(I) bonds and cation-π interaction with tryptophan, as reported for Ctr4, and a histidine residue in the Cys/Trp motif of Ctr5 is suggested to interact with Cu(I) via its Nτ atom. Ctr4 and Ctr5 exhibit a heterotrimeric form within cell membranes and the copper transport mechanism of the Ctr4/Ctr5 heterotrimer is discussed along with quantitative evaluation of the Cu(I)-binding constant of the Cys/Trp motif.
[Mh] Termos MeSH primário: Proteínas de Transporte de Cátions/química
Proteínas de Transporte de Cátions/metabolismo
Cobre/metabolismo
Metalochaperonas/química
Metalochaperonas/metabolismo
Proteínas de Schizosaccharomyces pombe/química
Proteínas de Schizosaccharomyces pombe/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos/fisiologia
Cobre/química
Cisteína/química
Modelos Biológicos
Domínios Proteicos/fisiologia
Triptofano/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cation Transport Proteins); 0 (Metallochaperones); 0 (Schizosaccharomyces pombe Proteins); 789U1901C5 (Copper); 8DUH1N11BX (Tryptophan); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170519
[Lr] Data última revisão:
170519
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170208
[St] Status:MEDLINE


  8 / 203 MEDLINE  
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[PMID]:28130442
[Au] Autor:Li Z; Kitanishi K; Twahir UT; Cracan V; Chapman D; Warncke K; Banerjee R
[Ad] Endereço:From the Department of Biological Chemistry, University of Michigan Medical Center, Ann Arbor, Michigan 48109-0600 and.
[Ti] Título:Cofactor Editing by the G-protein Metallochaperone Domain Regulates the Radical B Enzyme IcmF.
[So] Source:J Biol Chem;292(10):3977-3987, 2017 Mar 10.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:IcmF is a 5'-deoxyadenosylcobalamin (AdoCbl)-dependent enzyme that catalyzes the carbon skeleton rearrangement of isobutyryl-CoA to butyryl-CoA. It is a bifunctional protein resulting from the fusion of a G-protein chaperone with GTPase activity and the cofactor- and substrate-binding mutase domains with isomerase activity. IcmF is prone to inactivation during catalytic turnover, thus setting up its dependence on a cofactor repair system. Herein, we demonstrate that the GTPase activity of IcmF powers the ejection of the inactive cob(II)alamin cofactor and requires the presence of an acceptor protein, adenosyltransferase, for receiving it. Adenosyltransferase in turn converts cob(II)alamin to AdoCbl in the presence of ATP and a reductant. The repaired cofactor is then reloaded onto IcmF in a GTPase-gated step. The mechanistic details of cofactor loading and offloading from the AdoCbl-dependent IcmF are distinct from those of the better characterized and homologous methylmalonyl-CoA mutase/G-protein chaperone system.
[Mh] Termos MeSH primário: Acil Coenzima A/metabolismo
Proteínas de Bactérias/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Proteínas de Ligação ao GTP/metabolismo
Metalochaperonas/metabolismo
Vitamina B 12/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Cristalografia por Raios X
Metilmalonil-CoA Mutase/metabolismo
Modelos Moleculares
Chaperonas Moleculares/metabolismo
Domínios Proteicos
Transferases/metabolismo
Vitamina B 12/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Bacterial Proteins); 0 (Metallochaperones); 0 (Molecular Chaperones); 15621-60-0 (isobutyryl-coenzyme A); 2140-48-9 (butyryl-coenzyme A); EC 2.- (Transferases); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (GTP-Binding Proteins); EC 5.4.99.2 (Methylmalonyl-CoA Mutase); P6YC3EG204 (Vitamin B 12)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170727
[Lr] Data última revisão:
170727
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170129
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.775957


  9 / 203 MEDLINE  
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[PMID]:28107462
[Au] Autor:Schimo S; Wittig I; Pos KM; Ludwig B
[Ad] Endereço:Institute of Biochemistry, Membrane Transport Machineries, Goethe-University, Frankfurt am Main, Germany.
[Ti] Título:Cytochrome c Oxidase Biogenesis and Metallochaperone Interactions: Steps in the Assembly Pathway of a Bacterial Complex.
[So] Source:PLoS One;12(1):e0170037, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Biogenesis of mitochondrial cytochrome c oxidase (COX) is a complex process involving the coordinate expression and assembly of numerous subunits (SU) of dual genetic origin. Moreover, several auxiliary factors are required to recruit and insert the redox-active metal compounds, which in most cases are buried in their protein scaffold deep inside the membrane. Here we used a combination of gel electrophoresis and pull-down assay techniques in conjunction with immunostaining as well as complexome profiling to identify and analyze the composition of assembly intermediates in solubilized membranes of the bacterium Paracoccus denitrificans. Our results show that the central SUI passes through at least three intermediate complexes with distinct subunit and cofactor composition before formation of the holoenzyme and its subsequent integration into supercomplexes. We propose a model for COX biogenesis in which maturation of newly translated COX SUI is initially assisted by CtaG, a chaperone implicated in CuB site metallation, followed by the interaction with the heme chaperone Surf1c to populate the redox-active metal-heme centers in SUI. Only then the remaining smaller subunits are recruited to form the mature enzyme which ultimately associates with respiratory complexes I and III into supercomplexes.
[Mh] Termos MeSH primário: Complexo IV da Cadeia de Transporte de Elétrons/biossíntese
Metalochaperonas/metabolismo
Paracoccus denitrificans/metabolismo
[Mh] Termos MeSH secundário: Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Eletroforese em Gel de Poliacrilamida
Espectrometria de Massas
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Metallochaperones); EC 1.9.3.1 (Electron Transport Complex IV)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170810
[Lr] Data última revisão:
170810
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170121
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0170037


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[PMID]:28027931
[Au] Autor:Blockhuys S; Wittung-Stafshede P
[Ad] Endereço:Department Biology and Biological Engineering, Chalmers University of Technology, 412 96 Gothenburg, Sweden.
[Ti] Título:Copper chaperone Atox1 plays role in breast cancer cell migration.
[So] Source:Biochem Biophys Res Commun;483(1):301-304, 2017 Jan 29.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Copper (Cu) is an essential transition metal ion required as cofactor in many key enzymes. After cell uptake of Cu, the metal is transported by the cytoplasmic Cu chaperone Atox1 to P -type ATPases in the Golgi network for incorporation into Cu-dependent enzymes in the secretory path. Cu is vital for many steps of cancer progression and Atox1 was recently suggested to have additional functionality as a nuclear transcription factor. We here investigated the expression level, cellular localization and role in cell migration of Atox1 in an aggressive breast cancer cell line upon combining immunostaining, microscopy and a wound healing assay. We made the unexpected discovery that Atox1 accumulates at lamellipodia borders of migrating cancer cells and Atox1 silencing resulted in migration defects as evidenced from reduced wound closure. Therefore, we have discovered an unknown role of the Cu chaperone Atox1 in breast cancer cell migration.
[Mh] Termos MeSH primário: Neoplasias da Mama/metabolismo
Cobre/química
Regulação Neoplásica da Expressão Gênica
Metalochaperonas/metabolismo
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/metabolismo
Transporte Biológico
Proteínas de Transporte de Cátions/metabolismo
Linhagem Celular Tumoral
Movimento Celular
Progressão da Doença
Feminino
Inativação Gênica
Complexo de Golgi/metabolismo
Seres Humanos
Células MCF-7
Modelos Moleculares
Pseudópodes/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ATOX1 protein, human); 0 (Cation Transport Proteins); 0 (Metallochaperones); 789U1901C5 (Copper); EC 3.6.1.- (Adenosine Triphosphatases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170607
[Lr] Data última revisão:
170607
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161229
[St] Status:MEDLINE



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