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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]:29277319
[Au] Autor:Fan W; Guo Q; Liu C; Liu X; Zhang M; Long D; Xiang Z; Zhao A
[Ad] Endereço:State Key Laboratory of Silkworm Genome Biology, Key Laboratory of Sericultural Biology and Genetic Breeding, Ministry of Agriculture, Southwest University, Chongqing 400716, China.
[Ti] Título:Two mulberry phytochelatin synthase genes confer zinc/cadmium tolerance and accumulation in transgenic Arabidopsis and tobacco.
[So] Source:Gene;645:95-104, 2018 Mar 01.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Phytochelatin synthase (PCS) is an enzyme involved in the synthesis of phytochelatins, cysteine-rich peptides which play a key role in heavy metal (HM) detoxification of plants. Mulberry (Morus L.), one of the most ecologically and economically important tree genera, has the potential to remediate HM-contaminated soils. However, genes involved in HM detoxification in Morus, such as the PCS genes, have not been identified and characterized. In this study, we identified two Morus notabilis PCS genes based on a genome-wide analysis of the Morus genome database. Full-length MnPCS1 and MnPCS2 cDNAs were 1509 and 1491bp long, respectively. Quantitative real-time polymerase chain reaction (qRT-PCR) analysis revealed that, under 200µM Zn or either 30 or 100µM Cd stress, the relative expression of each of the two MaPCSs (from Morus alba) was induced in root, stem and leaf tissues within 24h of exposure to the metals, with Cd inducing expression more strongly than did Zn . Based on the analysis of total root length and fresh weight of seedlings, overexpression of MnPCS1 and MnPCS2 in Arabidopsis and tobacco enhanced Zn /Cd tolerance in most transgenic individuals. The results of transgenic Arabidopsis lines overexpressing MnPCS1and MnPCS2 suggest that MnPCS1 play a more important role in Cd detoxification than MnPCS2. Zn /Cd concentrations in both shoots and roots of the transgenic Arabidopsis seedlings were higher than in wild type (WT) seedlings at two Zn /Cd concentrations. In addition, there was a positive correlation between Zn accumulation and the expression level of MnPCS1 or MnPCS2. Our results indicated that the Morus PCS1 and PCS2 genes play important roles in HM stress tolerance and accumulation, providing a useful genetic resource for enhancing tolerance to HMs and for increasing the HM phytoremediation potential of these plants.
[Mh] Termos MeSH primário: Aminoaciltransferases/genética
Arabidopsis/genética
Morus/enzimologia
Tabaco/genética
[Mh] Termos MeSH secundário: Aminoaciltransferases/metabolismo
Arabidopsis/crescimento & desenvolvimento
Cádmio/metabolismo
Regulação da Expressão Gênica de Plantas
Morus/genética
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Raízes de Plantas/genética
Brotos de Planta/genética
Plantas Geneticamente Modificadas/crescimento & desenvolvimento
Estresse Fisiológico
Tabaco/crescimento & desenvolvimento
Zinco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); 00BH33GNGH (Cadmium); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.15 (glutathione gamma-glutamylcysteinyltransferase); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171227
[St] Status:MEDLINE


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[PMID]:29200433
[Au] Autor:Jeong HJ; Abhiraman GC; Story CM; Ingram JR; Dougan SK
[Ad] Endereço:Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Boston, Massachusetts, United States of America.
[Ti] Título:Generation of Ca2+-independent sortase A mutants with enhanced activity for protein and cell surface labeling.
[So] Source:PLoS One;12(12):e0189068, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sortase A, a calcium-dependent transpeptidase derived from Staphylococcus aureus, is used in a broad range of applications, such as the conjugation of fluorescent dyes and other moieties to proteins or to the surface of eukaryotic cells. In vivo and cell-based applications of sortase have been somewhat limited by the large range of calcium concentrations, as well as by the often transient nature of protein-protein interactions in living systems. In order to use sortase A for cell labeling applications, we generated a new sortase A variant by combining multiple mutations to yield an enzyme that was both calcium-independent and highly active. This variant has enhanced activity for both N- and C-terminal labeling, as well as for cell surface modification under physiological conditions.
[Mh] Termos MeSH primário: Aminoaciltransferases/genética
Proteínas de Bactérias/genética
Cálcio/metabolismo
Cisteína Endopeptidases/genética
Peptidil Transferases/genética
Coloração e Rotulagem/métodos
Staphylococcus aureus/genética
[Mh] Termos MeSH secundário: Aminoaciltransferases/metabolismo
Proteínas de Bactérias/metabolismo
Membrana Celular/química
Cisteína Endopeptidases/metabolismo
Mutação
Peptidil Transferases/metabolismo
Staphylococcus aureus/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.- (sortase A); EC 2.3.2.12 (Peptidyl Transferases); EC 3.4.22.- (Cysteine Endopeptidases); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189068


  4 / 1126 MEDLINE  
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[PMID]:28962862
[Au] Autor:Tamai E; Sekiya H; Maki J; Nariya H; Yoshida H; Kamitori S
[Ad] Endereço:Department of Infectious Disease, College of Pharmaceutical Science, Matsuyama University, 4-2 Bunkyo-cho, Matsuyama, Ehime 790-8578, Japan; Life Science Research Center and Faculty of Medicine, Kagawa University, 1750-1 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0793, Japan.
[Ti] Título:X-ray structure of Clostridium perfringens sortase B cysteine transpeptidase.
[So] Source:Biochem Biophys Res Commun;493(3):1267-1272, 2017 Nov 25.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The pathogenesis and infectivity of Gram-positive bacteria are mediated by many surface proteins that are covalently attached to peptidoglycans of the cell wall. The covalent attachment of these proteins is catalyzed by sortases (Srts), a family of cysteine transpeptidases, which are classified into six classes, A - F, based on their amino acid sequences and biological roles. Clostridium perfringens, one of the pathogenic clostridial species, has a class B sortase (CpSrtB) with 249 amino acid residues. X-ray structures of CpSrtB and its inactive mutant form were determined at 2.2 Å and 1.8 Å resolutions, respectively. CpSrtB adopts a typical sortase-protein fold, and has a unique substrate-binding groove formed by three ß-strands and two helices creating the sidewalls of the groove. The position of the catalytic Cys232 of CpSrtB is significantly different from those commonly found in Srts structures. The modeling study of the CpSrtB/peptide complex suggested that the position of Cys232 found in CpSrtB is preferable for the catalytic reaction to occur. Structural comparison with other class B sortases demonstrated that the catalytic site likely converts between two forms. The movement of Cys232 between the two forms may help His136 deprotonate Cys232 to be activated as a thiolate, which may the catalytic Cys-activated mechanism for Srts.
[Mh] Termos MeSH primário: Aminoaciltransferases/química
Aminoaciltransferases/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Clostridium perfringens/enzimologia
Cisteína Endopeptidases/química
Cisteína Endopeptidases/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Aminoaciltransferases/genética
Proteínas de Bactérias/genética
Sítios de Ligação
Domínio Catalítico
Cristalografia por Raios X
Cisteína/química
Cisteína/metabolismo
Cisteína Endopeptidases/genética
Modelos Moleculares
Mutação
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (sortase B); EC 2.3.2.- (Aminoacyltransferases); EC 3.4.22.- (Cysteine Endopeptidases); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171001
[St] Status:MEDLINE


  5 / 1126 MEDLINE  
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[PMID]:28893510
[Au] Autor:Gamage DG; Varma Y; Meitzler JL; Morissette R; Ness TJ; Hendrickson TL
[Ad] Endereço:Department of Chemistry, Wayne State University, 5101 Cass Avenue, Detroit, MI 48202, USA.
[Ti] Título:The soluble domains of Gpi8 and Gaa1, two subunits of glycosylphosphatidylinositol transamidase (GPI-T), assemble into a complex.
[So] Source:Arch Biochem Biophys;633:58-67, 2017 Nov 01.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glycosylphosphatidylinositol transamidase (GPI-T) catalyzes the post-translational addition of the GPI anchor to the C-terminus of some proteins. In most eukaryotes, Gpi8, the active site subunit of GPI-T, is part of a hetero-pentameric complex containing Gpi16, Gaa1, Gpi17, and Gab1. Gpi8, Gaa1, and Gpi16 co-purify as a heterotrimer from Saccharomyces cerevisiae, suggesting that they form the core of the GPI-T. Details about the assembly and organization of these subunits have been slow to emerge. We have previously shown that the soluble domain of S. cerevisiae Gpi8 (Gpi8 ) assembles as a homodimer, similar to the caspases with which it shares weak sequence homology (Meitzler, J. L. et al., 2007). Here we present the characterization of a complex between the soluble domains of Gpi8 and Gaa1. The complex between GST-Gpi8 (α) and His -Gaa1 (ß) was characterized by native gel analysis and size exclusion chromatography (SEC) and results are most consistent with an α ß stoichiometry. These results demonstrate that Gpi8 and Gaa1 interact specifically without a requirement for other subunits, bring us closer to determining the stoichiometry of the core subunits of GPI-T, and lend further credence to the hypothesis that these three subunits assemble into a dimer of a trimer.
[Mh] Termos MeSH primário: Aminoaciltransferases/química
Glicoproteínas de Membrana/química
Proteínas de Saccharomyces cerevisiae/química
Saccharomyces cerevisiae/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Aminoaciltransferases/genética
Aminoaciltransferases/metabolismo
Sítios de Ligação
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Cinética
Glicoproteínas de Membrana/genética
Glicoproteínas de Membrana/metabolismo
Modelos Moleculares
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Estrutura Terciária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Saccharomyces cerevisiae/enzimologia
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Solubilidade
Homologia Estrutural de Proteína
Especificidade por Substrato
Vibrionaceae/química
Vibrionaceae/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GAA1 protein, S cerevisiae); 0 (Membrane Glycoproteins); 0 (Recombinant Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.- (GPI8 protein, S cerevisiae)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170913
[St] Status:MEDLINE


  6 / 1126 MEDLINE  
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[PMID]:28859178
[Au] Autor:Suliman M; Santosh V; Seegar TCM; Dalton AC; Schultz KM; Klug CS; Barton WA
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Virginia Commonwealth University, Richmond, Virginia, United States of America.
[Ti] Título:Directed evolution provides insight into conformational substrate sampling by SrtA.
[So] Source:PLoS One;12(8):e0184271, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Sortase family of transpeptidases are found in numerous gram-positive bacteria and involved in divergent physiological processes including anchoring of surface proteins to the cell wall as well as pili assembly. As essential proteins, sortase enzymes have been the focus of considerable interest for the development of novel anti-microbials, however, more recently their function as unique transpeptidases has been exploited for the synthesis of novel bio-conjugates. Yet, for synthetic purposes, SrtA-mediated conjugation suffers from the enzyme's inherently poor catalytic efficiency. Therefore, to identify SrtA variants with improved catalytic efficiency, we used directed evolution to select a catalytically enhanced SrtA enzyme. An analysis of improved SrtA variants in the context of sequence conservation, NMR and x-ray crystal structures, and kinetic data suggests a novel mechanism for catalysis involving large conformational changes that delivers substrate to the active site pocket. Indeed, using DEER-EPR spectroscopy, we reveal that upon substrate binding, SrtA undergoes a large scissors-like conformational change that simultaneously translates the sort-tag substrate to the active site in addition to repositioning key catalytic residues for esterification. A better understanding of Sortase dynamics will significantly enhance future engineering and drug discovery efforts.
[Mh] Termos MeSH primário: Aminoaciltransferases/química
Proteínas de Bactérias/química
Cisteína Endopeptidases/química
Evolução Molecular Direcionada
Staphylococcus aureus/enzimologia
[Mh] Termos MeSH secundário: Aminoaciltransferases/genética
Aminoaciltransferases/metabolismo
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Catálise
Domínio Catalítico
Cristalografia por Raios X
Cisteína Endopeptidases/genética
Cisteína Endopeptidases/metabolismo
Espectroscopia de Ressonância de Spin Eletrônica
Cinética
Conformação Proteica
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.- (sortase A); EC 3.4.22.- (Cysteine Endopeptidases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171011
[Lr] Data última revisão:
171011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184271


  7 / 1126 MEDLINE  
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[PMID]:28859130
[Au] Autor:Balachandran M; Giannone RJ; Bemis DA; Kania SA
[Ad] Endereço:Department of Biomedical and Diagnostic Sciences, The University of Tennessee, Knoxville, Tennessee, United States of America.
[Ti] Título:Molecular basis of surface anchored protein A deficiency in the Staphylococcus aureus strain Wood 46.
[So] Source:PLoS One;12(8):e0183913, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein A in Staphylococcus aureus is encoded by the spa (staphylococcal protein A) gene and binds to immunoglobulin (Ig). The S. aureus strain Wood 46 has been variously reported as protein A-deficient and/or spa negative and used as a control in animal models of staphylococcal infections. The results of this study indicate that Wood 46 has normal spa expression but transcribes very low levels of the srtA gene which encodes the sortase A (SrtA) enzyme. This is consistent with unique mutations in the srtA promoter. In this study, a low level of sortase A explains deficient anchoring of proteins with an LPXTG motif, such as protein A, fibrinogen-binding protein and fibronectin-binding proteins A and B on to the peptidoglycan cell wall. The activity of secreted protein A is an important consideration for use of Wood 46 in functional experiments and animal models.
[Mh] Termos MeSH primário: Adesinas Bacterianas/genética
Aminoaciltransferases/genética
Proteínas de Bactérias/genética
Proteínas de Transporte/genética
Cisteína Endopeptidases/genética
Regulação Bacteriana da Expressão Gênica
Proteína Estafilocócica A/genética
Staphylococcus aureus/genética
[Mh] Termos MeSH secundário: Adesinas Bacterianas/metabolismo
Motivos de Aminoácidos
Aminoaciltransferases/metabolismo
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Proteínas de Transporte/metabolismo
Parede Celular/química
Parede Celular/metabolismo
Cisteína Endopeptidases/metabolismo
Mutação
Regiões Promotoras Genéticas
Ligação Proteica
Proteína Estafilocócica A/metabolismo
Staphylococcus aureus/metabolismo
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Bacterial Proteins); 0 (Carrier Proteins); 0 (Staphylococcal Protein A); 0 (fibrinogen-binding protein A, Staphylococcus aureus); 0 (fibronectin-binding proteins, bacterial); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.- (sortase A); EC 3.4.22.- (Cysteine Endopeptidases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183913


  8 / 1126 MEDLINE  
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[PMID]:28844905
[Au] Autor:Wang J; Pavlyk I; Vedula P; Sterling S; Leu NA; Dong DW; Kashina A
[Ad] Endereço:University of Pennsylvania, School of Veterinary Medicine, Philadelphia, PA 19104, United States.
[Ti] Título:Arginyltransferase ATE1 is targeted to the neuronal growth cones and regulates neurite outgrowth during brain development.
[So] Source:Dev Biol;430(1):41-51, 2017 10 01.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Arginylation is an emerging protein modification mediated by arginyltransferase ATE1, shown to regulate embryogenesis and actin cytoskeleton, however its functions in different physiological systems are not well understood. Here we analyzed the role of ATE1 in brain development and neuronal growth by producing a conditional mouse knockout with Ate1 deletion in the nervous system driven by Nestin promoter (Nes-Ate1 mice). These mice were weaker than wild type, resulting in low postnatal survival rates, and had abnormalities in the brain that suggested defects in neuronal migration. Cultured Ate1 knockout neurons showed a reduction in the neurite outgrowth and the levels of doublecortin and F-actin in the growth cones. In wild type, ATE1 prominently localized to the growth cones, in addition to the cell bodies. Examination of the Ate1 mRNA sequence reveals the existence of putative zipcode-binding sequences involved in mRNA targeting to the cell periphery and local translation at the growth cones. Fluorescence in situ hybridization showed that Ate1 mRNA localized to the tips of the growth cones, likely due to zipcode-mediated targeting, and this localization coincided with spots of localization of arginylated ß-actin, which disappeared in the presence of protein synthesis inhibitors. We propose that zipcode-mediated co-targeting of Ate1 and ß-actin mRNA leads to localized co-translational arginylation of ß-actin that drives the growth cone migration and neurite outgrowth.
[Mh] Termos MeSH primário: Aminoaciltransferases/metabolismo
Encéfalo/crescimento & desenvolvimento
Encéfalo/metabolismo
Cones de Crescimento/enzimologia
Neuritos/enzimologia
Crescimento Neuronal
[Mh] Termos MeSH secundário: Actinas/metabolismo
Animais
Arginina/metabolismo
Encéfalo/anormalidades
Encéfalo/patologia
Movimento Celular
Camundongos Endogâmicos C57BL
Camundongos Knockout
Camundongos Transgênicos
Proteínas Associadas aos Microtúbulos/metabolismo
Modelos Biológicos
Neuropeptídeos/metabolismo
Biossíntese de Proteínas
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Actins); 0 (Microtubule-Associated Proteins); 0 (Neuropeptides); 0 (RNA, Messenger); 0 (doublecortin protein); 94ZLA3W45F (Arginine); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.8 (arginyltransferase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170829
[St] Status:MEDLINE


  9 / 1126 MEDLINE  
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[PMID]:28764927
[Au] Autor:Calendar R
[Ad] Endereço:Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA. Electronic address: rishard@berkeley.edu.
[Ti] Título:d-Tyrosyl-tRNA Deacylase: A New Function.
[So] Source:Trends Biochem Sci;42(9):684-686, 2017 Sep.
[Is] ISSN:0968-0004
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:d-Aminoacyl-tRNA deacylase (DTD) hydrolyzes d-amino acids mistakenly attached to tRNAs and, thus, has been implicated in perpetuating protein homochirality. Fifty years after the discovery of DTD, it has now been shown that its function extends beyond 'chiral proofreading' because it also eliminates glycine that has been erroneously coupled to tRNA .
[Mh] Termos MeSH primário: Aminoaciltransferases/metabolismo
[Mh] Termos MeSH secundário: Escherichia coli/enzimologia
Glicina/metabolismo
RNA de Transferência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9014-25-9 (RNA, Transfer); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.- (D-tyrosine tRNA(Tyr) deacylase); TE7660XO1C (Glycine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171011
[Lr] Data última revisão:
171011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE


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[PMID]:28756135
[Au] Autor:Srinivasan S; Hazra JP; Singaraju GS; Deb D; Rakshit S
[Ad] Endereço:Department of Chemical Sciences, Indian Institute of Science Education and Research, Mohali, Punjab, 140306, India.
[Ti] Título:ESCORTing proteins directly from whole cell-lysate for single-molecule studies.
[So] Source:Anal Biochem;535:35-42, 2017 Oct 15.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We have developed a method for Enzymatic Sortase-assisted Covalent Orientation-specific Restraint Tethering (ESCORT) recombinant proteins onto surfaces directly from cell-lysate. With an improved surface passivation method, we obviate the cumbersome purification steps even for single molecule studies that demand high purity in the sample. We demonstrated high-specificity of the method, high-passivity of the surface and uncompromised functional integrity of anchored proteins using single molecule fluorescence and force-mapping. We anticipate that this method will substantially reduce the investment by way of time, money and energy in the area of single molecule studies.
[Mh] Termos MeSH primário: Aminoaciltransferases/metabolismo
Proteínas de Bactérias/metabolismo
Extratos Celulares/química
Cisteína Endopeptidases/metabolismo
Imagem Individual de Molécula/métodos
Staphylococcus aureus/citologia
[Mh] Termos MeSH secundário: Proteínas Recombinantes/metabolismo
Staphylococcus aureus/metabolismo
Propriedades de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cell Extracts); 0 (Recombinant Proteins); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.- (sortase A); EC 3.4.22.- (Cysteine Endopeptidases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170731
[St] Status:MEDLINE



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