Base de dados : MEDLINE
Pesquisa : D08.811.464 [Categoria DeCS]
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  1 / 8773 MEDLINE  
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[PMID]:28461174
[Au] Autor:Dalonso N; Savoldi M; França PHC; Reis TF; Goldman GH; Gern RMM
[Ad] Endereço:Programa de Pós Graduação em Saúde e Meio Ambiente, Universidade da Região de Joinville, UNIVILLE, Joinville, SC 89201-972, Brazil. Electronic address: nenidalo@yahoo.com.br.
[Ti] Título:Sequence-independent cloning methods for long DNA fragments applied to synthetic biology.
[So] Source:Anal Biochem;530:5-8, 2017 08 01.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Simplified methods to assemble DNA fragments by independent cloning sequence have helped in the progress of synthetic biology, allowing some biotechnological processes to become economically viable by genetic improvement of microorganisms. We compared three methods of assembling six DNA fragments: PCR fusion-based, isothermal NEBuilder and circular polymerase extension cloning (CPEC). Double and triple fusion occurs directly with the PCR products using PCR fusion-based and NEBuilder methods. For multiple fragments the results showed higher efficiency by the CPEC method which allowed assembly of six fragments previously purified by agarose gel extraction, after a sequence of 20 annealing/extension cycles without any primer.
[Mh] Termos MeSH primário: Clonagem Molecular/métodos
DNA/química
DNA/genética
Reação em Cadeia da Polimerase/métodos
Biologia Sintética/métodos
[Mh] Termos MeSH secundário: Ligases/metabolismo
Transformação Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
9007-49-2 (DNA); EC 6.- (Ligases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


  2 / 8773 MEDLINE  
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[PMID]:28740167
[Au] Autor:Soria-Bretones I; Cepeda-García C; Checa-Rodriguez C; Heyer V; Reina-San-Martin B; Soutoglou E; Huertas P
[Ad] Endereço:Departamento de Genética, Universidad de Sevilla, Sevilla, 41080, Spain.
[Ti] Título:DNA end resection requires constitutive sumoylation of CtIP by CBX4.
[So] Source:Nat Commun;8(1):113, 2017 07 24.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:DNA breaks are complex DNA lesions that can be repaired by two alternative mechanisms: non-homologous end-joining and homologous recombination. The decision between them depends on the activation of the DNA resection machinery, which blocks non-homologous end-joining and stimulates recombination. On the other hand, post-translational modifications play a critical role in DNA repair. We have found that the SUMO E3 ligase CBX4 controls resection through the key factor CtIP. Indeed, CBX4 depletion impairs CtIP constitutive sumoylation and DNA end processing. Importantly, mutating lysine 896 in CtIP recapitulates the CBX4-depletion phenotype, blocks homologous recombination and increases genomic instability. Artificial fusion of CtIP and SUMO suppresses the effects of both the non-sumoylatable CtIP mutant and CBX4 depletion. Mechanistically, CtIP sumoylation is essential for its recruitment to damaged DNA. In summary, sumoylation of CtIP at lysine 896 defines a subpopulation of the protein that is involved in DNA resection and recombination.The choice between non-homologous end-joining and homologous recombination to repair a DNA double-strand break depends on activation of the end resection machinery. Here the authors show that SUMO E3 ligase CBX4 sumoylates subpopulation of CtIP to regulate recruitment to breaks and resection.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Quebras de DNA de Cadeia Dupla
Reparo do DNA por Junção de Extremidades
Ligases/metabolismo
Proteínas Nucleares/metabolismo
Proteínas do Grupo Polycomb/metabolismo
[Mh] Termos MeSH secundário: Western Blotting
Proteínas de Transporte/genética
Linhagem Celular Tumoral
DNA/genética
DNA/metabolismo
Células HEK293
Recombinação Homóloga
Seres Humanos
Ligases/genética
Microscopia Confocal
Proteínas Nucleares/genética
Proteínas do Grupo Polycomb/genética
Interferência de RNA
Proteína SUMO-1/genética
Proteína SUMO-1/metabolismo
Proteínas Modificadoras Pequenas Relacionadas à Ubiquitina/genética
Proteínas Modificadoras Pequenas Relacionadas à Ubiquitina/metabolismo
Sumoilação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Nuclear Proteins); 0 (Polycomb-Group Proteins); 0 (RBBP8 protein, human); 0 (SUMO-1 Protein); 0 (SUMO1 protein, human); 0 (SUMO2 protein, human); 0 (Small Ubiquitin-Related Modifier Proteins); 9007-49-2 (DNA); EC 6.- (Ligases); EC 6.3.2.- (CBX4 protein, human)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-00183-6


  3 / 8773 MEDLINE  
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[PMID]:28991254
[Au] Autor:Teh BT; Lim K; Yong CH; Ng CCY; Rao SR; Rajasegaran V; Lim WK; Ong CK; Chan K; Cheng VKY; Soh PS; Swarup S; Rozen SG; Nagarajan N; Tan P
[Ad] Endereço:Thorn Biosystems Pte Ltd, Singapore.
[Ti] Título:The draft genome of tropical fruit durian (Durio zibethinus).
[So] Source:Nat Genet;49(11):1633-1641, 2017 Nov.
[Is] ISSN:1546-1718
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Durian (Durio zibethinus) is a Southeast Asian tropical plant known for its hefty, spine-covered fruit and sulfury and onion-like odor. Here we present a draft genome assembly of D. zibethinus, representing the third plant genus in the Malvales order and first in the Helicteroideae subfamily to be sequenced. Single-molecule sequencing and chromosome contact maps enabled assembly of the highly heterozygous durian genome at chromosome-scale resolution. Transcriptomic analysis showed upregulation of sulfur-, ethylene-, and lipid-related pathways in durian fruits. We observed paleopolyploidization events shared by durian and cotton and durian-specific gene expansions in MGL (methionine γ-lyase), associated with production of volatile sulfur compounds (VSCs). MGL and the ethylene-related gene ACS (aminocyclopropane-1-carboxylic acid synthase) were upregulated in fruits concomitantly with their downstream metabolites (VSCs and ethylene), suggesting a potential association between ethylene biosynthesis and methionine regeneration via the Yang cycle. The durian genome provides a resource for tropical fruit biology and agronomy.
[Mh] Termos MeSH primário: Bombacaceae/genética
Liases de Carbono-Enxofre/genética
Frutas/genética
Genoma de Planta
Proteínas de Plantas/genética
Transcriptoma
[Mh] Termos MeSH secundário: Aminoácidos Cíclicos/biossíntese
Bombacaceae/classificação
Bombacaceae/crescimento & desenvolvimento
Bombacaceae/metabolismo
Liases de Carbono-Enxofre/metabolismo
Mapeamento Cromossômico
Frutas/crescimento & desenvolvimento
Frutas/metabolismo
Sequenciamento de Nucleotídeos em Larga Escala
Ligases/genética
Ligases/metabolismo
Metabolismo dos Lipídeos/genética
Filogenia
Proteínas de Plantas/metabolismo
Enxofre/metabolismo
Compostos Orgânicos Voláteis/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids, Cyclic); 0 (Plant Proteins); 0 (Volatile Organic Compounds); 3K9EJ633GL (1-aminocyclopropane-1-carboxylic acid); 70FD1KFU70 (Sulfur); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.11 (L-methionine gamma-lyase); EC 6.- (Ligases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171010
[St] Status:MEDLINE
[do] DOI:10.1038/ng.3972


  4 / 8773 MEDLINE  
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[PMID]:28834007
[Au] Autor:Witzgall F; Ewert W; Blankenfeldt W
[Ad] Endereço:Structure and Function of Proteins, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, 38124, Braunschweig, Germany.
[Ti] Título:Structures of the N-Terminal Domain of PqsA in Complex with Anthraniloyl- and 6-Fluoroanthraniloyl-AMP: Substrate Activation in Pseudomonas Quinolone Signal (PQS) Biosynthesis.
[So] Source:Chembiochem;18(20):2045-2055, 2017 Oct 18.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Pseudomonas aeruginosa, a prevalent pathogen in nosocomial infections and a major burden in cystic fibrosis, uses three interconnected quorum-sensing systems to coordinate virulence processes. At variance with other Gram-negative bacteria, one of these systems relies on 2-alkyl-4(1H)-quinolones (Pseudomonas quinolone signal, PQS) and might hence be an attractive target for new anti-infective agents. Here we report crystal structures of the N-terminal domain of anthranilate-CoA ligase PqsA, the first enzyme of PQS biosynthesis, in complex with anthraniloyl-AMP and with 6-fluoroanthraniloyl-AMP (6FABA-AMP) at 1.4 and 1.7 Šresolution. We find that PqsA belongs to an unrecognized subfamily of anthranilate-CoA ligases that recognize the amino group of anthranilate through a water-mediated hydrogen bond. The complex with 6FABA-AMP explains why 6FABA, an inhibitor of PQS biosynthesis, is a good substrate of PqsA. Together, our data might pave a way to new pathoblockers in P. aeruginosa infections.
[Mh] Termos MeSH primário: Ligases/química
Ligases/metabolismo
Pseudomonas aeruginosa/citologia
Pseudomonas aeruginosa/metabolismo
Quinolonas/metabolismo
Percepção de Quorum
ortoaminobenzoatos/metabolismo
[Mh] Termos MeSH secundário: Domínio Catalítico
Cristalografia por Raios X
Modelos Moleculares
Pseudomonas aeruginosa/enzimologia
ortoaminobenzoatos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Quinolones); 0 (ortho-Aminobenzoates); 0YS975XI6W (anthranilic acid); EC 6.- (Ligases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170824
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700374


  5 / 8773 MEDLINE  
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[PMID]:28809541
[Au] Autor:Puvar K; Zhou Y; Qiu J; Luo ZQ; Wirth MJ; Das C
[Ad] Endereço:Department of Chemistry, Purdue University , 560 Oval Drive, West Lafayette, Indiana 47906, United States.
[Ti] Título:Ubiquitin Chains Modified by the Bacterial Ligase SdeA Are Protected from Deubiquitinase Hydrolysis.
[So] Source:Biochemistry;56(36):4762-4766, 2017 Sep 12.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The SidE family of Legionella pneumophila effectors is a unique group of ubiquitin-modifying enzymes. Along with catalyzing NAD -dependent ubiquitination of certain host proteins independent of the canonical E1/E2/E3 pathway, they have also been shown to produce phosphoribosylated free ubiquitin. This modified ubiquitin product is incompatible with conventional E1/E2/E3 ubiquitination processes, with the potential to lock down various cellular functions that are dependent on ubiquitin signaling. Here, we show that in addition to free ubiquitin, Lys63-, Lys48-, Lys11-, and Met1-linked diubiquitin chains are also modified by SdeA in a similar fashion. Both the proximal and distal ubiquitin moieties are targeted in the phosphoribosylation reaction. Furthermore, this renders the ubiquitin chains unable to be processed by a variety of deubiquitinating enzymes. These observations broaden the scope of SdeA's modulatory functions during Legionella infection.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Enzimas Desubiquitinantes/metabolismo
Legionella pneumophila/enzimologia
Ligases/metabolismo
Ubiquitina/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Enzimas Desubiquitinantes/genética
Regulação Bacteriana da Expressão Gênica
Regulação Enzimológica da Expressão Gênica
Hidrólise
Ligases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Ubiquitin); EC 3.4.19.12 (Deubiquitinating Enzymes); EC 6.- (Ligases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170816
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00664


  6 / 8773 MEDLINE  
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[PMID]:28712727
[Au] Autor:Karaduman R; Chanarat S; Pfander B; Jentsch S
[Ad] Endereço:Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried, Germany. Electronic address: karaduma@biochem.mpg.de.
[Ti] Título:Error-Prone Splicing Controlled by the Ubiquitin Relative Hub1.
[So] Source:Mol Cell;67(3):423-432.e4, 2017 Aug 03.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Accurate pre-mRNA splicing is needed for correct gene expression and relies on faithful splice site recognition. Here, we show that the ubiquitin-like protein Hub1 binds to the DEAD-box helicase Prp5, a key regulator of early spliceosome assembly, and stimulates its ATPase activity thereby enhancing splicing and relaxing fidelity. High Hub1 levels enhance splicing efficiency but also cause missplicing by tolerating suboptimal splice sites and branchpoint sequences. Notably, Prp5 itself is regulated by a Hub1-dependent negative feedback loop. Since Hub1-mediated splicing activation induces cryptic splicing of Prp5, it also represses Prp5 protein levels and thus curbs excessive missplicing. Our findings indicate that Hub1 mediates enhanced, but error-prone splicing, a mechanism that is tightly controlled by a feedback loop of PRP5 cryptic splicing activation.
[Mh] Termos MeSH primário: Ligases/metabolismo
Precursores de RNA/metabolismo
Sítios de Splice de RNA
Processamento de RNA
RNA Fúngico/metabolismo
RNA Mensageiro/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
Spliceossomos/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Sítios de Ligação
RNA Helicases DEAD-box/genética
RNA Helicases DEAD-box/metabolismo
Retroalimentação Fisiológica
Regulação Fúngica da Expressão Gênica
Hidrólise
Ligases/química
Ligases/genética
Modelos Moleculares
Mutação
Ligação Proteica
Conformação Proteica
Precursores de RNA/genética
RNA Fúngico/genética
RNA Mensageiro/genética
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Spliceossomos/genética
Relação Estrutura-Atividade
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA Precursors); 0 (RNA Splice Sites); 0 (RNA, Fungal); 0 (RNA, Messenger); 0 (Saccharomyces cerevisiae Proteins); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (PRP5 protein, S cerevisiae); EC 3.6.4.13 (DEAD-box RNA Helicases); EC 6.- (Ligases); EC 6.3.2.- (HUB1 protein, S cerevisiae)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE


  7 / 8773 MEDLINE  
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[PMID]:28672070
[Au] Autor:Singal B; Balakrishna AM; Nartey W; Manimekalai MSS; Jeyakanthan J; Grüber G
[Ad] Endereço:School of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
[Ti] Título:Crystallographic and solution structure of the N-terminal domain of the Rel protein from Mycobacterium tuberculosis.
[So] Source:FEBS Lett;591(15):2323-2337, 2017 Aug.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Modulation of intracellular guanosine 3',5'-bispyrophosphate ((p)ppGpp) level, the effector of the stringent response, is crucial for survival as well as optimal growth of prokaryotes and, thus, for bacterial pathogenesis and dormancy. In Mycobacterium tuberculosis (Mtb), (p)ppGpp synthesis and degradation are carried out by the bifunctional enzyme MtRel, which consists of 738 residues, including an N-terminal hydrolase- and synthetase-domain (N-terminal domain or NTD) and a C-terminus with a ribosome-binding site. Here, we present the first crystallographic structure of the enzymatically active MtRel NTD determined at 3.7 Å resolution. The structure provides insights into the residues of MtRel NTD responsible for nucleotide binding. Small-angle X-ray scattering experiments were performed to investigate the dimeric state of the MtRel NTD and possible substrate-dependent structural alterations.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Mycobacterium tuberculosis/química
Pirofosfatases/química
Pirofosfatases/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Cromatografia Líquida de Alta Pressão
Cristalografia por Raios X
Ligases/química
Ligases/genética
Ligases/metabolismo
Conformação Proteica
Domínios Proteicos
Multimerização Proteica
Pirofosfatases/genética
Espalhamento a Baixo Ângulo
Difração de Raios X
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 3.6.1.- (Pyrophosphatases); EC 6.- (Ligases); EC 6.- (guanosine 3',5'-polyphosphate synthetases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170704
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12739


  8 / 8773 MEDLINE  
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[PMID]:28666590
[Au] Autor:Kanao R; Masutani C
[Ad] Endereço:Department of Genome Dynamics, Research Institute of Environmental Medicine, Nagoya University, Nagoya, Japan.
[Ti] Título:Regulation of DNA damage tolerance in mammalian cells by post-translational modifications of PCNA.
[So] Source:Mutat Res;803-805:82-88, 2017 Oct.
[Is] ISSN:1873-135X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:DNA damage tolerance pathways, which include translesion DNA synthesis (TLS) and template switching, are crucial for prevention of DNA replication arrest and maintenance of genomic stability. However, these pathways utilize error-prone DNA polymerases or template exchange between sister DNA strands, and consequently have the potential to induce mutations or chromosomal rearrangements. Post-translational modifications of proliferating cell nuclear antigen (PCNA) play important roles in controlling these pathways. For example, TLS is mediated by mono-ubiquitination of PCNA at lysine 164, for which RAD6-RAD18 is the primary E2-E3 complex. Elaborate protein-protein interactions between mono-ubiquitinated PCNA and Y-family DNA polymerases constitute the core of the TLS regulatory system, and enhancers of PCNA mono-ubiquitination and de-ubiquitinating enzymes finely regulate TLS and suppress TLS-mediated mutagenesis. The template switching pathway is promoted by K63-linked poly-ubiquitination of PCNA at lysine 164. Poly-ubiquitination is achieved by a coupled reaction mediated by two sets of E2-E3 complexes, RAD6-RAD18 and MMS2-UBC13-HTLF/SHPRH. In addition to these mono- and poly-ubiquitinations, simultaneous mono-ubiquitinations on multiple units of the PCNA homotrimeric ring promote an unidentified damage tolerance mechanism that remains to be fully characterized. Furthermore, SUMOylation of PCNA in mammalian cells can negatively regulate recombination. Other modifications, including ISGylation, acetylation, methylation, or phosphorylation, may also play roles in DNA damage tolerance and control of genomic stability.
[Mh] Termos MeSH primário: Dano ao DNA
Antígeno Nuclear de Célula em Proliferação/genética
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Animais
DNA Helicases/genética
DNA Helicases/metabolismo
Replicação do DNA
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/metabolismo
DNA Polimerase Dirigida por DNA/genética
DNA Polimerase Dirigida por DNA/metabolismo
Fatores de Transcrição Forkhead/genética
Fatores de Transcrição Forkhead/metabolismo
Regulação da Expressão Gênica
Instabilidade Genômica
Seres Humanos
Ligases/genética
Ligases/metabolismo
Mutagênese
Antígeno Nuclear de Célula em Proliferação/metabolismo
Sumoilação
Enzimas de Conjugação de Ubiquitina/genética
Enzimas de Conjugação de Ubiquitina/metabolismo
Ubiquitina-Proteína Ligases/genética
Ubiquitina-Proteína Ligases/metabolismo
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (FOXN2 protein, human); 0 (Forkhead Transcription Factors); 0 (Proliferating Cell Nuclear Antigen); EC 2.3.2.23 (UBE2N protein, human); EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes); EC 2.3.2.27 (SHPRH protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.7.7.7 (DNA-Directed DNA Polymerase); EC 3.6.4.- (DNA Helicases); EC 6.- (Ligases); EC 6.3.2.19 (RAD18 protein, human); EC 6.3.2.19 (UBE2V2 protein, human)
[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:170702
[St] Status:MEDLINE


  9 / 8773 MEDLINE  
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[PMID]:28633319
[Au] Autor:Zhang BZ; Cai J; Yu B; Xiong L; Lin Q; Yang XY; Xu C; Zheng S; Kao RY; Sze K; Yuen KY; Huang JD
[Ad] Endereço:School of Biomedical Sciences.
[Ti] Título:Immunotherapy Targeting Adenosine Synthase A Decreases Severity of Staphylococcus aureus Infection in Mouse Model.
[So] Source:J Infect Dis;216(2):245-253, 2017 Jul 15.
[Is] ISSN:1537-6613
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Staphylococcusaureus is a severe pathogen found in the community and in hospitals. Most notably, methicillin-resistant S. aureus (MRSA) is resistant to almost all antibiotics, which is a growing public health concern. The emergence of drug-resistant strains has prompted the search for alternative treatments such as immunotherapeutic approaches. Previous research showed that S. aureus exploit the immunomodulatory attributes of adenosine to escape host immunity. In this study, we investigated adenosine synthase A (AdsA), an S. aureus cell wall-anchored enzyme as possible targets for immunotherapy. Mice vaccinated with aluminum hydroxide-formulated recombinant AdsA (rAdsA) induced high-titer anti-AdsA antibodies, thereby providing consistent protection in 3 mouse infection models when challenged with 2 S. aureus strains. The importance of anti-AdsA antibody in protection was demonstrated by passive transfer experiments. Moreover, AdsA-specific antisera promote killing S. aureus by immune cells. Altogether, our data demonstrate that the AdsA is a promising target for vaccines and therapeutics development to alleviate severe S. aureus diseases.
[Mh] Termos MeSH primário: Anticorpos Antibacterianos/farmacologia
Proteínas de Bactérias/imunologia
Imunização Passiva
Ligases/imunologia
Infecções Cutâneas Estafilocócicas/terapia
[Mh] Termos MeSH secundário: Adenosina/biossíntese
Animais
Antibacterianos/uso terapêutico
Modelos Animais de Doenças
Feminino
Imunoterapia
Camundongos
Camundongos Endogâmicos BALB C
Coelhos
Staphylococcus aureus/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Antibodies, Bacterial); 0 (Bacterial Proteins); EC 6.- (Ligases); K72T3FS567 (Adenosine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.1093/infdis/jix290


  10 / 8773 MEDLINE  
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[PMID]:28604693
[Au] Autor:Luo X; Fu G; Wang RE; Zhu X; Zambaldo C; Liu R; Liu T; Lyu X; Du J; Xuan W; Yao A; Reed SA; Kang M; Zhang Y; Guo H; Huang C; Yang PY; Wilson IA; Schultz PG; Wang F
[Ad] Endereço:Department of Chemistry, The Scripps Research Institute, La Jolla, California, USA.
[Ti] Título:Genetically encoding phosphotyrosine and its nonhydrolyzable analog in bacteria.
[So] Source:Nat Chem Biol;13(8):845-849, 2017 Aug.
[Is] ISSN:1552-4469
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tyrosine phosphorylation is a common protein post-translational modification that plays a critical role in signal transduction and the regulation of many cellular processes. Using a propeptide strategy to increase cellular uptake of O-phosphotyrosine (pTyr) and its nonhydrolyzable analog 4-phosphomethyl-L-phenylalanine (Pmp), we identified an orthogonal aminoacyl-tRNA synthetase-tRNA pair that allows site-specific incorporation of both pTyr and Pmp into recombinant proteins in response to the amber stop codon in Escherichia coli in good yields. The X-ray structure of the synthetase reveals a reconfigured substrate-binding site, formed by nonconservative mutations and substantial local structural perturbations. We demonstrate the utility of this method by introducing Pmp into a putative phosphorylation site and determining the affinities of the individual variants for the substrate 3BP2. In summary, this work provides a useful recombinant tool to dissect the biological functions of tyrosine phosphorylation at specific sites in the proteome.
[Mh] Termos MeSH primário: Códon sem Sentido/genética
Escherichia coli/genética
Escherichia coli/metabolismo
Fosfotirosina/análogos & derivados
Fosfotirosina/genética
[Mh] Termos MeSH secundário: Cristalografia por Raios X
Ligases/química
Ligases/metabolismo
Modelos Moleculares
Estrutura Molecular
Fosforilação
Fosfotirosina/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon, Nonsense); 0 (Recombinant Proteins); 21820-51-9 (Phosphotyrosine); EC 6.- (Ligases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170613
[St] Status:MEDLINE
[do] DOI:10.1038/nchembio.2405



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