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  1 / 216206 MEDLINE  
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[PMID]:29346419
[Au] Autor:Holcomb J; Doughan M; Spellmon N; Lewis B; Perry E; Zhang Y; Nico L; Wan J; Chakravarthy S; Shang W; Miao Q; Stemmler T; Yang Z
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, Michigan, United States of America.
[Ti] Título:SAXS analysis of a soluble cytosolic NgBR construct including extracellular and transmembrane domains.
[So] Source:PLoS One;13(1):e0191371, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Nogo-B receptor (NgBR) is involved in oncogenic Ras signaling through directly binding to farnesylated Ras. It recruits farnesylated Ras to the non-lipid-raft membrane for interaction with downstream effectors. However, the cytosolic domain of NgBR itself is only partially folded. The lack of several conserved secondary structural elements makes this domain unlikely to form a complete farnesyl binding pocket. We find that inclusion of the extracellular and transmembrane domains that contain additional conserved residues to the cytosolic region results in a well folded protein with a similar size and shape to the E.coli cis-isoprenyl transferase (UPPs). Small Angle X-ray Scattering (SAXS) analysis reveals the radius of gyration (Rg) of our NgBR construct to be 18.2 Å with a maximum particle dimension (Dmax) of 61.0 Å. Ab initio shape modeling returns a globular molecular envelope with an estimated molecular weight of 23.0 kD closely correlated with the calculated molecular weight. Both Kratky plot and pair distribution function of NgBR scattering reveal a bell shaped peak which is characteristic of a single globularly folded protein. In addition, circular dichroism (CD) analysis reveals that our construct has the secondary structure contents similar to the UPPs. However, this result does not agree with the currently accepted topological orientation of NgBR which might partition this construct into three separate domains. This discrepancy suggests another possible NgBR topology and lends insight into a potential molecular basis of how NgBR facilitates farnesylated Ras recruitment.
[Mh] Termos MeSH primário: Receptores de Superfície Celular/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Membrana Celular/metabolismo
Dicroísmo Circular
Citosol/metabolismo
Peso Molecular
Estrutura Secundária de Proteína
Receptores de Superfície Celular/metabolismo
Espalhamento a Baixo Ângulo
Homologia de Sequência de Aminoácidos
Solubilidade
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (NUS1 protein, human); 0 (Receptors, Cell Surface)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180119
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191371


  2 / 216206 MEDLINE  
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[PMID]:29339159
[Au] Autor:Popinako A; Antonov M; Dibrova D; Chemeris A; Sokolova OS
[Ad] Endereço:A.N. Bach Institute of Biochemistry, Research Center of Biotechnology of RAS, 33 Leninsky Ave, bld. 2, Moscow, 119071, Russia.
[Ti] Título:Analysis of the interactions between GMF and Arp2/3 complex in two binding sites by molecular dynamics simulation.
[So] Source:Biochem Biophys Res Commun;496(2):529-535, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Arp2/3 complex plays a key role in nucleating actin filaments branching. The glia maturation factor (GMF) competes with activators for interacting with the Arp2/3 complex and initiates the debranching of actin filaments. In this study, we performed a comparative analysis of interactions between GMF and the Arp2/3 complex and identified new amino acid residues involved in GMF binding to the Arp2/3 complex at two separate sites, revealed by X-ray and single particle EM techniques. Using molecular dynamics simulations we demonstrated the quantitative and qualitative changes in hydrogen bonds upon binding with GMF. We identified the specific amino acid residues in GMF and Arp2/3 complex that stabilize the interactions and estimated the mean force profile for the GMF using umbrella sampling. Phylogenetic and structural analyses of the recently defined GMF binding site on the Arp3 subunit indicate a new mechanism for Arp2/3 complex inactivation that involves interactions between the Arp2/3 complex and GMF at two binding sites.
[Mh] Termos MeSH primário: Complexo 2-3 de Proteínas Relacionadas à Actina/metabolismo
Fator de Maturação da Glia/metabolismo
[Mh] Termos MeSH secundário: Complexo 2-3 de Proteínas Relacionadas à Actina/química
Animais
Sítios de Ligação
Bovinos
Cristalografia por Raios X
Fator de Maturação da Glia/química
Camundongos
Simulação de Dinâmica Molecular
Ligação Proteica
Mapas de Interação de Proteínas
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actin-Related Protein 2-3 Complex); 0 (Glia Maturation Factor)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE


  3 / 216206 MEDLINE  
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[PMID]:29221486
[Au] Autor:Suzuki T; Maeda S; Furuhata E; Shimizu Y; Nishimura H; Kishima M; Suzuki H
[Ad] Endereço:Division of Genomic Technologies, RIKEN Center for Life Science Technologies (CLST), RIKEN Yokohama Campus, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama City, Kanagawa, 230-0045, Japan.
[Ti] Título:A screening system to identify transcription factors that induce binding site-directed DNA demethylation.
[So] Source:Epigenetics Chromatin;10(1):60, 2017 12 08.
[Is] ISSN:1756-8935
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: DNA methylation is a fundamental epigenetic modification that is involved in many biological systems such as differentiation and disease. We and others recently showed that some transcription factors (TFs) are involved in the site-specific determination of DNA demethylation in a binding site-directed manner, although the reports of such TFs are limited. RESULTS: Here, we develop a screening system to identify TFs that induce binding site-directed DNA methylation changes. The system involves the ectopic expression of target TFs in model cells followed by DNA methylome analysis and overrepresentation analysis of the corresponding TF binding motif at differentially methylated regions. It successfully identified binding site-directed demethylation of SPI1, which is known to promote DNA demethylation in a binding site-directed manner. We extended our screening system to 15 master TFs involved in cellular differentiation and identified eight novel binding site-directed DNA demethylation-inducing TFs (RUNX3, GATA2, CEBPB, MAFB, NR4A2, MYOD1, CEBPA, and TBX5). Gene ontology and tissue enrichment analysis revealed that these TFs demethylate genomic regions associated with corresponding biological roles. We also describe the characteristics of binding site-directed DNA demethylation induced by these TFs, including the targeting of highly methylated CpGs, local DNA demethylation, and the overlap of demethylated regions between TFs of the same family. CONCLUSIONS: Our results show the usefulness of the developed screening system for the identification of TFs that induce DNA demethylation in a site-directed manner.
[Mh] Termos MeSH primário: Desmetilação
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Metilação de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Transcription Factors)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180310
[Lr] Data última revisão:
180310
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171210
[St] Status:MEDLINE
[do] DOI:10.1186/s13072-017-0169-6


  4 / 216206 MEDLINE  
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[PMID]:29175397
[Au] Autor:Dong G; Huang L; Wu X; Wang C; Liu Y; Liu G; Wang L; Liu X; Xia H
[Ad] Endereço:Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering, Shandong University, Jinan, 250100, China. Electronic address: 963722867@qq.com.
[Ti] Título:Effect and mechanism analysis of MnO on permeable reactive barrier (PRB) system for the removal of tetracycline.
[So] Source:Chemosphere;193:702-710, 2018 Feb.
[Is] ISSN:1879-1298
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Effect of manganese dioxide (MnO ) on tetracycline (TC) removal/degradation in zero-valent iron (ZVI) based permeable reactive barrier (PRB) system was investigated. To analyze the role of MnO , three different PRB columns packed with ZVI, ZVI and a layer of MnO , and MnO were set up to investigate the removal effect and reaction mechanism of ZVI coupling with MnO on TC removal, respectively. The results show that the removal efficiencies of three PRB columns are 65%, 85%, and 50%, respectively. MnO could accelerate the transformation of Fe into Fe and combine with Fe to degrade TC in different reaction sites in the ZVI-MnO PRB system. Hydroxyl radicals (·OH) were produced in this process, which contributed to about 58.3% for the TC degradation. The UV-Vis spectrum demonstrated that A ring of TC was the main reaction site for interaction with Fe and the BCD rings were crucial for interactions with MnO . On the basis of intermediates identified by LC-ESI-MS, the ring structure of TC was opened, and low-molecular-weight compounds were produced in ZVI-MnO PRB system.
[Mh] Termos MeSH primário: Ferro/química
Compostos de Manganês/farmacologia
Óxidos/farmacologia
Tetraciclina/isolamento & purificação
[Mh] Termos MeSH secundário: Sítios de Ligação
Cromatografia Líquida
Estrutura Molecular
Espectrometria de Massas em Tandem
Tetraciclina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Manganese Compounds); 0 (Oxides); E1UOL152H7 (Iron); F8VB5M810T (Tetracycline); TF219GU161 (manganese dioxide)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE


  5 / 216206 MEDLINE  
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[PMID]:28466911
[Au] Autor:Scheller JS; Irvine GW; Wong DL; Hartwig A; Stillman MJ
[Ad] Endereço:Department of Chemistry, The University of Western Ontario, London, Ontario, N6A 5B7, Canada. martin.stillman@uwo.ca.
[Ti] Título:Stepwise copper(i) binding to metallothionein: a mixed cooperative and non-cooperative mechanism for all 20 copper ions.
[So] Source:Metallomics;9(5):447-462, 2017 May 24.
[Is] ISSN:1756-591X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Copper is a ubiquitous trace metal of vital importance in that it serves as a cofactor in many metalloenzymes. Excess copper becomes harmful if not sequestered appropriately in the cell. As a metal ion chaperone, metallothionein (MT) has been proposed as a key player in zinc and copper homeostasis within the cell. The underlying mechanisms by which MT sequesters and transfers copper ions, and subsequently achieves its proposed biological function remain unknown. Using a combination of electrospray ionization mass spectrometry (ESI-MS), circular dichroism (CD), and emission spectroscopy, we report that the Cu(i) to human apo-MT1a binding mechanism is highly pH-dependent. The 20 relative K -values for the binding of 1 to 20 Cu(i) to the 20 cysteines of MT were obtained from computational simulation of the experimental mass spectral results. These data identified the pH-dependent formation of three sequential but completely different Cu-S clusters, as a function of Cu(i) loading. These data provide the first overall sequence for Cu(i) binding in terms of domain specificity and transient binding site structures. Under cooperative binding at pH 7.4, a series of four clusters form: Cu S , followed by Cu S (ß), then a second Cu S (α), and finally Cu S (α) (x = up to 11). Upon further addition of Cu(i), a mixture of species is formed in a non-cooperative mechanism, saturating the 20 cysteines of MT1a. Using benzoquinone, a cysteine modifier, we were able to confirm that Cu S formed solely in the N-terminal ß-domain, as well as confirming the existence of the presumed Cu S cluster in the α-domain. Based on the results of ESI-MS and computational simulation we were able to identify Cu:MT speciation that resulted in specific emission and CD spectral properties.
[Mh] Termos MeSH primário: Cobre/metabolismo
Metalotioneína/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Dicroísmo Circular
Cobre/química
Seres Humanos
Concentração de Íons de Hidrogênio
Metalotioneína/química
Modelos Moleculares
Ligação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Espectrometria de Massas por Ionização por Electrospray
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MT1A protein, human); 0 (Recombinant Proteins); 789U1901C5 (Copper); 9038-94-2 (Metallothionein)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1039/c7mt00041c


  6 / 216206 MEDLINE  
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[PMID]:28463568
[Au] Autor:Salinas G; Gao W; Wang Y; Bonilla M; Yu L; Novikov A; Virginio VG; Ferreira HB; Vieites M; Gladyshev VN; Gambino D; Dai S
[Ad] Endereço:1 Worm Biology Lab, Institut Pasteur de Montevideo , Montevideo, Uruguay .
[Ti] Título:The Enzymatic and Structural Basis for Inhibition of Echinococcus granulosus Thioredoxin Glutathione Reductase by Gold(I).
[So] Source:Antioxid Redox Signal;27(18):1491-1504, 2017 Dec 20.
[Is] ISSN:1557-7716
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:AIMS: New drugs are needed to treat flatworm infections that cause severe human diseases such as schistosomiasis. The unique flatworm enzyme thioredoxin glutathione reductase (TGR), structurally different from the human enzyme, is a key drug target. Structural studies of the flatworm Echinococcus granulosus TGR, free and complexed with Au -MPO, a novel gold inhibitor, together with inhibition assays were performed. RESULTS: Au -MPO is a potent TGR inhibitor that achieves 75% inhibition at a 1:1 TGR:Au ratio and efficiently kills E. granulosus in vitro. The structures revealed salient insights: (i) unique monomer-monomer interactions, (ii) distinct binding sites for thioredoxin and the glutaredoxin (Grx) domain, (iii) a single glutathione disulfide reduction site in the Grx domain, (iv) rotation of the Grx domain toward the Sec-containing redox active site, and (v) a single gold atom bound to Cys and Cys in the Au -TGR complex. Structural modeling suggests that these residues are involved in the stabilization of the Sec-containing C-terminus. Consistently, Cys→Ser mutations in these residues decreased TGR activities. Mass spectroscopy confirmed these cysteines are the primary binding site. INNOVATION: The identification of a primary site for gold binding and the structural model provide a basis for gold compound optimization through scaffold adjustments. CONCLUSIONS: The structural study revealed that TGR functions are achieved not only through a mobile Sec-containing redox center but also by rotation of the Grx domain and distinct binding sites for Grx domain and thioredoxin. The conserved Cys and Cys residues targeted by gold assist catalysis through stabilization of the Sec-containing redox center. Antioxid. Redox Signal. 27, 1491-1504.
[Mh] Termos MeSH primário: Echinococcus granulosus/enzimologia
Complexos Multienzimáticos/química
Complexos Multienzimáticos/metabolismo
NADH NADPH Oxirredutases/química
NADH NADPH Oxirredutases/metabolismo
Compostos Organoáuricos/farmacologia
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação/efeitos dos fármacos
Cisteína/metabolismo
Echinococcus granulosus/química
Echinococcus granulosus/genética
Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacocinética
Glutarredoxinas/metabolismo
Proteínas de Helminto/química
Proteínas de Helminto/genética
Proteínas de Helminto/metabolismo
Modelos Moleculares
Complexos Multienzimáticos/genética
Mutação
NADH NADPH Oxirredutases/genética
Compostos Organoáuricos/química
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Glutaredoxins); 0 (Helminth Proteins); 0 (Multienzyme Complexes); 0 (Organogold Compounds); EC 1.6.- (NADH, NADPH Oxidoreductases); EC 1.6.4.- (thioredoxin glutathione reductase); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1089/ars.2016.6816


  7 / 216206 MEDLINE  
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[PMID]:29182018
[Au] Autor:Amin SA; Adhikari N; Jha T
[Ad] Endereço:Natural Science Laboratory, Department of Pharmaceutical Technology, Division of Medicinal & Pharmaceutical Chemistry, PO Box 17020, Jadavpur University, Kolkata 700032, West Bengal, India.
[Ti] Título:Structure-activity relationships of hydroxamate-based histone deacetylase-8 inhibitors: reality behind anticancer drug discovery.
[So] Source:Future Med Chem;9(18):2211-2237, 2017 12.
[Is] ISSN:1756-8927
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The pan-histone deacetylase (HDAC) inhibitors comprise a fish-like structural orientation where hydrophobic aryl- and zinc-binding groups act as head and tail, respectively of a fish. The linker moiety correlates the body of the fish linking head and tail groups. Despite these pan-HDAC inhibitors, selective HDAC-8 inhibitors are still in demand as a safe remedy. HDAC-8 is involved in invasion and metastasis in cancer. This review deals with the rationale behind HDAC-8 inhibitory activity and selectivity along with detailed structure-activity relationships of diverse hydroxamate-based HDAC-8 inhibitors. HDAC-8 inhibitory potency may be increased by modifying the fish-like pharmacophoric features of such type of pan-HDAC inhibitors. This review may provide a preliminary basis to design and optimize new lead molecules with higher HDAC-8 inhibitory activity. This work may surely enlighten in providing useful information in the field of target-specific anticancer therapy.
[Mh] Termos MeSH primário: Antineoplásicos/química
Inibidores de Histona Desacetilases/química
Ácidos Hidroxâmicos/química
Proteínas Repressoras/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/uso terapêutico
Sítios de Ligação
Desenho de Drogas
Inibidores de Histona Desacetilases/uso terapêutico
Histona Desacetilases/metabolismo
Seres Humanos
Ácidos Hidroxâmicos/uso terapêutico
Simulação de Acoplamento Molecular
Neoplasias/tratamento farmacológico
Neoplasias/patologia
Proteínas Repressoras/metabolismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Histone Deacetylase Inhibitors); 0 (Hydroxamic Acids); 0 (Repressor Proteins); EC 3.5.1.98 (HDAC8 protein, human); EC 3.5.1.98 (Histone Deacetylases)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171129
[St] Status:MEDLINE
[do] DOI:10.4155/fmc-2017-0130


  8 / 216206 MEDLINE  
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[PMID]:29172693
[Au] Autor:Ojeda-Montes MJ; Ardid-Ruiz A; Tomás-Hernández S; Gimeno A; Cereto-Massagué A; Beltrán-Debón R; Mulero M; Garcia-Vallvé S; Pujadas G; Valls C
[Ad] Endereço:Research group in Cheminformatics & Nutrition, Departament de Bioquímica i Biotecnologia, Universitat Rovira i Virgili, Campus de Sescelades, Tarragona, Catalonia 43007, Spain.
[Ti] Título:Ephedrine as a lead compound for the development of new DPP-IV inhibitors.
[So] Source:Future Med Chem;9(18):2129-2146, 2017 12.
[Is] ISSN:1756-8927
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIM: Extracts from Ephedra species have been reported to be effective as antidiabetics. A previous in silico study predicted that ephedrine and five ephedrine derivatives could contribute to the described antidiabetic effect of Ephedra extracts by inhibiting dipeptidyl peptidase IV (DPP-IV). Finding selective DPP-IV inhibitors is a current therapeutic strategy for Type 2 diabetes mellitus management. Therefore, the main aim of this work is to experimentally determine whether these alkaloids are DPP-IV inhibitors. Materials & methods: The DPP-IV inhibition of Ephedra's alkaloids was determined via a competitive-binding assay. Then, computational analyses were used in order to find out the protein-ligand interactions and to perform a lead optimization. RESULTS: Our results show that all six molecules are DPP-IV inhibitors, with IC ranging from 124 µM for ephedrine to 28 mM for N-methylpseudoephedrine. CONCLUSION: Further computational analysis shows how Ephedra's alkaloids could be used as promising lead molecules for designing more potent and selective DPP-IV inhibitors.
[Mh] Termos MeSH primário: Dipeptidil Peptidase 4/metabolismo
Inibidores da Dipeptidil Peptidase IV/química
Efedrina/análogos & derivados
Hipoglicemiantes/química
[Mh] Termos MeSH secundário: Alcaloides/química
Alcaloides/metabolismo
Sítios de Ligação
Ligação Competitiva
Dipeptidil Peptidase 4/química
Desenho de Drogas
Ephedra/química
Ephedra/metabolismo
Efedrina/metabolismo
Hipoglicemiantes/metabolismo
Concentração Inibidora 50
Simulação de Acoplamento Molecular
Fenilpropanolamina/química
Extratos Vegetais/química
Isoformas de Proteínas/antagonistas & inibidores
Isoformas de Proteínas/metabolismo
Estrutura Terciária de Proteína
Estereoisomerismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Alkaloids); 0 (Dipeptidyl-Peptidase IV Inhibitors); 0 (Hypoglycemic Agents); 0 (Plant Extracts); 0 (Protein Isoforms); 33RU150WUN (Phenylpropanolamine); EC 3.4.14.5 (Dipeptidyl Peptidase 4); GN83C131XS (Ephedrine)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.4155/fmc-2017-0080


  9 / 216206 MEDLINE  
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[PMID]:29410408
[Au] Autor:Kuncha SK; Mazeed M; Singh R; Kattula B; Routh SB; Sankaranarayanan R
[Ad] Endereço:CSIR-Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad, 500007, India.
[Ti] Título:A chiral selectivity relaxed paralog of DTD for proofreading tRNA mischarging in Animalia.
[So] Source:Nat Commun;9(1):511, 2018 02 06.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:D-aminoacyl-tRNA deacylase (DTD), a bacterial/eukaryotic trans-editing factor, removes D-amino acids mischarged on tRNAs and achiral glycine mischarged on tRNA . An invariant cross-subunit Gly-cisPro motif forms the mechanistic basis of L-amino acid rejection from the catalytic site. Here, we present the identification of a DTD variant, named ATD (Animalia-specific tRNA deacylase), that harbors a Gly-transPro motif. The cis-to-trans switch causes a "gain of function" through L-chiral selectivity in ATD resulting in the clearing of L-alanine mischarged on tRNA (G4•U69) by eukaryotic AlaRS. The proofreading activity of ATD is conserved across diverse classes of phylum Chordata. Animalia genomes enriched in tRNA (G4•U69) genes are in strict association with the presence of ATD, underlining the mandatory requirement of a dedicated factor to proofread tRNA misaminoacylation. The study highlights the emergence of ATD during genome expansion as a key event associated with the evolution of Animalia.
[Mh] Termos MeSH primário: Alanina/química
Aminoaciltransferases/química
Aminoacil-RNA de Transferência/química
Treonina/química
Aminoacilação de RNA de Transferência/genética
[Mh] Termos MeSH secundário: Alanina/genética
Alanina/metabolismo
Sequência de Aminoácidos
Aminoaciltransferases/genética
Aminoaciltransferases/metabolismo
Animais
Apicomplexa/genética
Apicomplexa/metabolismo
Bactérias/genética
Bactérias/metabolismo
Sítios de Ligação
Evolução Biológica
Clonagem Molecular
Cristalografia por Raios X
Expressão Gênica
Seres Humanos
Modelos Moleculares
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Aminoacil-RNA de Transferência/genética
Aminoacil-RNA de Transferência/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
Treonina/genética
Treonina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Transfer, Amino Acyl); 0 (Recombinant Proteins); 2ZD004190S (Threonine); EC 2.3.2.- (Aminoacyltransferases); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180208
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02204-w


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[PMID]:29220449
[Au] Autor:Choi JA; Wyrick JJ
[Ad] Endereço:School of Molecular Biosciences.
[Ti] Título:RegulatorDB: a resource for the analysis of yeast transcriptional regulation.
[So] Source:Database (Oxford);2017, 2017 Jan 01.
[Is] ISSN:1758-0463
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Database URL: http://wyrickbioinfo2.smb.wsu.edu/RegulatorDB.
[Mh] Termos MeSH primário: DNA Fúngico
Proteínas de Ligação a DNA
Bases de Dados Genéticas
Proteínas Fúngicas
Regulação Fúngica da Expressão Gênica/genética
Saccharomyces cerevisiae
[Mh] Termos MeSH secundário: Sítios de Ligação
DNA Fúngico/genética
DNA Fúngico/metabolismo
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/metabolismo
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Fungal); 0 (DNA-Binding Proteins); 0 (Fungal Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE
[do] DOI:10.1093/database/bax058



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