Base de dados : MEDLINE
Pesquisa : D08.811.150.280.250 [Categoria DeCS]
Referências encontradas : 224 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 23 ir para página                         

  1 / 224 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28180279
[Au] Autor:Cooper LP; Roberts GA; White JH; Luyten YA; Bower EKM; Morgan RD; Roberts RJ; Lindsay JA; Dryden DTF
[Ad] Endereço:EaStCHEM School of Chemistry, University of Edinburgh, The King's Buildings, Edinburgh, EH9 3FJ, UK.
[Ti] Título:DNA target recognition domains in the Type I restriction and modification systems of Staphylococcus aureus.
[So] Source:Nucleic Acids Res;45(6):3395-3406, 2017 Apr 07.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Staphylococcus aureus displays a clonal population structure in which horizontal gene transfer between different lineages is extremely rare. This is due, in part, to the presence of a Type I DNA restriction-modification (RM) system given the generic name of Sau1, which maintains different patterns of methylation on specific target sequences on the genomes of different lineages. We have determined the target sequences recognized by the Sau1 Type I RM systems present in a wide range of the most prevalent S. aureus lineages and assigned the sequences recognized to particular target recognition domains within the RM enzymes. We used a range of biochemical assays on purified enzymes and single molecule real-time sequencing on genomic DNA to determine these target sequences and their patterns of methylation. Knowledge of the main target sequences for Sau1 will facilitate the synthesis of new vectors for transformation of the most prevalent lineages of this 'untransformable' bacterium.
[Mh] Termos MeSH primário: Metilases de Modificação do DNA/química
Metilases de Modificação do DNA/metabolismo
Desoxirribonucleases de Sítio Específico do Tipo I/química
Desoxirribonucleases de Sítio Específico do Tipo I/metabolismo
Staphylococcus aureus/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
DNA/química
DNA/metabolismo
Domínios Proteicos
Análise de Sequência de DNA
Staphylococcus aureus/genética
Transformação Bacteriana
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9007-49-2 (DNA); EC 2.1.1.- (DNA Modification Methylases); EC 3.1.21.3 (Deoxyribonucleases, Type I Site-Specific)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170210
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx067


  2 / 224 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27654959
[Au] Autor:Koyama R; Arai T; Kijima M; Sato S; Miura S; Yuasa M; Kitamura D; Mizuta R
[Ad] Endereço:Research Institute for Biomedical Sciences, Tokyo University of Science, 2669 Yamazaki, Noda, Chiba, 278-0022, Japan.
[Ti] Título:DNase γ, DNase I and caspase-activated DNase cooperate to degrade dead cells.
[So] Source:Genes Cells;21(11):1150-1163, 2016 Nov.
[Is] ISSN:1365-2443
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Serum endonucleases are essential for degrading the chromatin released from dead cells and preventing autoimmune diseases such as systemic lupus erythematosus. Serum DNase I is known as the major endonuclease, but recently, another endonuclease, DNase γ/DNase I-like 3, gained attention. However, the precise role of each endonuclease, especially that of DNase γ, remains unclear. In this study, we distinguished the activities of DNase γ from those of DNase I in mouse serum and concluded that both cooperated in degrading DNA during necrosis: DNase γ functions as the primary chromatolytic activity, causing internucleosomal DNA fragmentation, and DNase I as the secondary one, causing random DNA digestion for its complete degradation. These results were confirmed by two in vivo experimental mouse models, in which necrosis was induced, acetaminophen-induced hepatic injury and streptozotocin-induced ß-cell necrosis models. We also determined that DNase γ functions as a backup endonuclease for caspase-activated DNase (CAD) in the secondary necrosis phase after γ-ray-induced apoptosis in vivo.
[Mh] Termos MeSH primário: Degradação Necrótica do DNA
Desoxirribonucleases de Sítio Específico do Tipo I/sangue
Desoxirribonucleases/sangue
Endodesoxirribonucleases/sangue
[Mh] Termos MeSH secundário: Animais
Apoptose
Linhagem Celular Tumoral
Fragmentação do DNA
Feminino
Seres Humanos
Fígado/metabolismo
Fígado/ultraestrutura
Masculino
Camundongos
Camundongos Knockout
Complexos Multienzimáticos
Necrose/sangue
Proteínas de Ligação a Poli-ADP-Ribose
Baço/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Multienzyme Complexes); 0 (Poly-ADP-Ribose Binding Proteins); 0 (aposome); EC 3.1.- (Deoxyribonucleases); EC 3.1.- (Dffb protein, mouse); EC 3.1.- (Endodeoxyribonucleases); EC 3.1.- (casepase-activated DNase, mouse); EC 3.1.- (deoxyribonuclease gamma); EC 3.1.21.3 (Deoxyribonucleases, Type I Site-Specific)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160923
[St] Status:MEDLINE
[do] DOI:10.1111/gtc.12433


  3 / 224 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27506595
[Au] Autor:Grottesi A; Cecconi S; Molina R; D'abramo M
[Ad] Endereço:SuperComputing Applications and Innovations, CINECA, via dei Tizii 6, Rome, 00185, Italy.
[Ti] Título:Effect of DNA on the conformational dynamics of the endonucleases I-DmoI as provided by molecular dynamics simulations.
[So] Source:Biopolymers;105(12):898-904, 2016 Dec.
[Is] ISSN:1097-0282
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The conformational behavior of the wild-type endonucleases I-DmoI and two of its mutants has been studied in the presence and in the absence of DNA target sequences by means of extended molecular dynamics simulations. Our results show that in the absence of DNA, the three protein forms explore a similar essential conformational space, whereas when bound to the same DNA target sequence of 25 base pairs, they diversify and restrain the subspace explored. In addition, the differences in the essential subspaces explored by the residues near the catalytic site for both the bound and unbound forms are discussed in background of the experimental protein activity.
[Mh] Termos MeSH primário: DNA/química
Desoxirribonucleases de Sítio Específico do Tipo I/química
Simulação de Dinâmica Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9007-49-2 (DNA); EC 3.1.21.- (endodeoxyribonuclease I-Dmo I); EC 3.1.21.3 (Deoxyribonucleases, Type I Site-Specific)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170206
[Lr] Data última revisão:
170206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160811
[St] Status:MEDLINE
[do] DOI:10.1002/bip.22933


  4 / 224 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27193539
[Au] Autor:Chen K; Stephanou AS; Roberts GA; White JH; Cooper LP; Houston PJ; Lindsay JA; Dryden DT
[Ad] Endereço:EaStCHEM School of Chemistry, University of Edinburgh the King's Buildings, Edinburgh, EH9 3JJ, UK.
[Ti] Título:The Type I Restriction Enzymes as Barriers to Horizontal Gene Transfer: Determination of the DNA Target Sequences Recognised by Livestock-Associated Methicillin-Resistant Staphylococcus aureus Clonal Complexes 133/ST771 and 398.
[So] Source:Adv Exp Med Biol;915:81-97, 2016.
[Is] ISSN:0065-2598
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Type I DNA restriction-modification (RM) systems of Staphylococcus aureus are known to act as a significant barrier to horizontal gene transfer between S. aureus strains belonging to different clonal complexes. The livestock-associated clonal complexes CC133/771 and CC398 contain Type I RM systems not found in human MRSA strains as yet but at some point transfer will occur. When this does take place, horizontal gene transfer of resistance will happen more easily between these strains. The reservoir of antibiotic resistance, virulence and host-adaptation genes present in livestock-associated MRSA will then potentially contribute to the development of newly evolving MRSA clones. The target sites recognised by the Type I RM systems of CC133/771 and CC398 were identified as CAG(N)5RTGA and ACC(N)5RTGA, respectively. Assuming that these enzymes recognise the methylation state of adenine, the underlined A and T bases indicate the unique positions of methylation. Target methylation points for enzymes from CC1 were also identified. The methylation points for CC1-1 are CCAY(N)5TTAA and those for CC1-2 are CCAY(N)6 TGT with the underline indicating the adenine methylation site thus clearing up the ambiguity noted previously (Roberts et al. 2013, Nucleic Acids Res 41:7472-7484) for the half sites containing two adenine bases.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
DNA Bacteriano/metabolismo
Desoxirribonucleases de Sítio Específico do Tipo I/metabolismo
Transferência Genética Horizontal
Gado/microbiologia
Staphylococcus aureus Resistente à Meticilina/enzimologia
Leite/microbiologia
Infecções Estafilocócicas/microbiologia
[Mh] Termos MeSH secundário: Adenina/metabolismo
Sequência de Aminoácidos
Animais
Antibacterianos/farmacologia
Proteínas de Bactérias/genética
Sequência de Bases
Bovinos
Metilação de DNA
DNA Bacteriano/genética
Desoxirribonucleases de Sítio Específico do Tipo I/genética
Farmacorresistência Bacteriana/genética
Genótipo
Interações Hospedeiro-Patógeno
Staphylococcus aureus Resistente à Meticilina/efeitos dos fármacos
Staphylococcus aureus Resistente à Meticilina/genética
Staphylococcus aureus Resistente à Meticilina/isolamento & purificação
Dados de Sequência Molecular
Fenótipo
Infecções Estafilocócicas/tratamento farmacológico
Infecções Estafilocócicas/transmissão
Especificidade por Substrato
Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (DNA, Bacterial); EC 3.1.21.3 (Deoxyribonucleases, Type I Site-Specific); JAC85A2161 (Adenine)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:161109
[Lr] Data última revisão:
161109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160520
[St] Status:MEDLINE
[do] DOI:10.1007/978-3-319-32189-9_7


  5 / 224 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26909878
[Au] Autor:Molina R; Besker N; Marcaida MJ; Montoya G; Prieto J; D'Abramo M
[Ad] Endereço:Structural Biology and Biocomputing Programme, Macromolecular Crystallography Group, Spanish National Cancer Research Centre (CNIO) , c/Melchor Fdez. Almagro 3, 28029 Madrid, Spain.
[Ti] Título:Key Players in I-DmoI Endonuclease Catalysis Revealed from Structure and Dynamics.
[So] Source:ACS Chem Biol;11(5):1401-7, 2016 05 20.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Homing endonucleases, such as I-DmoI, specifically recognize and cleave long DNA target sequences (∼20 bp) and are potentially powerful tools for genome manipulation. However, inefficient and off-target DNA cleavage seriously limits specific editing in complex genomes. One approach to overcome these limitations is to unambiguously identify the key structural players involved in catalysis. Here, we report the E117A I-DmoI mutant crystal structure at 2.2 Šresolution that, together with the wt and Q42A/K120M constructs, is combined with computational approaches to shed light on protein cleavage activity. The cleavage mechanism was related both to key structural effects, such as the position of water molecules and ions participating in the cleavage reaction, and to dynamical effects related to protein behavior. In particular, we found that the protein perturbation pattern significantly changes between cleaved and noncleaved DNA strands when the ions and water molecules are correctly positioned for the nucleophilic attack that initiates the cleavage reaction, in line with experimental enzymatic activity. The proposed approach paves the way for an effective, general, and reliable procedure to analyze the enzymatic activity of endonucleases from a very limited data set, i.e., structure and dynamics.
[Mh] Termos MeSH primário: Desoxirribonucleases de Sítio Específico do Tipo I/química
Desoxirribonucleases de Sítio Específico do Tipo I/metabolismo
Desulfurococcaceae/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Domínio Catalítico
Cristalografia por Raios X
DNA/metabolismo
Desoxirribonucleases de Sítio Específico do Tipo I/genética
Desulfurococcaceae/química
Desulfurococcaceae/metabolismo
Simulação de Dinâmica Molecular
Mutação Puntual
Conformação Proteica
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
9007-49-2 (DNA); EC 3.1.21.- (endodeoxyribonuclease I-Dmo I); EC 3.1.21.3 (Deoxyribonucleases, Type I Site-Specific)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170404
[Lr] Data última revisão:
170404
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160225
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.5b00730


  6 / 224 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26568416
[Au] Autor:Yüksel D; Bianco PR; Kumar K
[Ad] Endereço:Department of Chemistry, Tufts University, 62 Talbot Avenue, Medford, MA 02155, USA. krishna.kumar@tufts.edu.
[Ti] Título:De novo design of protein mimics of B-DNA.
[So] Source:Mol Biosyst;12(1):169-77, 2016 Jan.
[Is] ISSN:1742-2051
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Structural mimicry of DNA is utilized in nature as a strategy to evade molecular defences mounted by host organisms. One such example is the protein Ocr - the first translation product to be expressed as the bacteriophage T7 infects E. coli. The structure of Ocr reveals an intricate and deliberate arrangement of negative charges that endows it with the ability to mimic ∼24 base pair stretches of B-DNA. This uncanny resemblance to DNA enables Ocr to compete in binding the type I restriction modification (R/M) system, and neutralizes the threat of hydrolytic cleavage of viral genomic material. Here, we report the de novo design and biophysical characterization of DNA mimicking peptides, and describe the inhibitory action of the designed helical bundles on a type I R/M enzyme, EcoR124I. This work validates the use of charge patterning as a design principle for creation of protein mimics of DNA, and serves as a starting point for development of therapeutic peptide inhibitors against human pathogens that employ molecular camouflage as part of their invasion stratagem.
[Mh] Termos MeSH primário: DNA de Forma B/química
Mimetismo Molecular
Proteínas/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
DNA de Forma B/metabolismo
Desoxirribonucleases de Sítio Específico do Tipo I/química
Desoxirribonucleases de Sítio Específico do Tipo I/metabolismo
Modelos Moleculares
Conformação Molecular
Dados de Sequência Molecular
Peptídeos/química
Peptídeos/metabolismo
Ligação Proteica
Proteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (DNA, B-Form); 0 (Peptides); 0 (Proteins); EC 3.1.21.3 (Deoxyribonucleases, Type I Site-Specific)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:170101
[Lr] Data última revisão:
170101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151117
[St] Status:MEDLINE
[do] DOI:10.1039/c5mb00524h


  7 / 224 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26045557
[Au] Autor:Molina R; Marcaida MJ; Redondo P; Marenchino M; Duchateau P; D'Abramo M; Montoya G; Prieto J
[Ad] Endereço:From the Macromolecular Crystallography Group and.
[Ti] Título:Engineering a Nickase on the Homing Endonuclease I-DmoI Scaffold.
[So] Source:J Biol Chem;290(30):18534-44, 2015 Jul 24.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Homing endonucleases are useful tools for genome modification because of their capability to recognize and cleave specifically large DNA targets. These endonucleases generate a DNA double strand break that can be repaired by the DNA damage response machinery. The break can be repaired by homologous recombination, an error-free mechanism, or by non-homologous end joining, a process susceptible to introducing errors in the repaired sequence. The type of DNA cleavage might alter the balance between these two alternatives. The use of "nickases" producing a specific single strand break instead of a double strand break could be an approach to reduce the toxicity associated with non-homologous end joining by promoting the use of homologous recombination to repair the cleavage of a single DNA break. Taking advantage of the sequential DNA cleavage mechanism of I-DmoI LAGLIDADG homing endonuclease, we have developed a new variant that is able to cut preferentially the coding DNA strand, generating a nicked DNA target. Our structural and biochemical analysis shows that by decoupling the action of the catalytic residues acting on each strand we can inhibit one of them while keeping the other functional.
[Mh] Termos MeSH primário: Desoxirribonuclease I/química
Desoxirribonucleases de Sítio Específico do Tipo I/química
Marcação de Genes
Engenharia de Proteínas
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Domínio Catalítico
Dicroísmo Circular
Cristalografia por Raios X
Quebras de DNA de Cadeia Dupla
Reparo do DNA por Junção de Extremidades/genética
Proteínas de Ligação a DNA/química
Proteínas de Ligação a DNA/genética
Desoxirribonuclease I/genética
Desoxirribonuclease I/metabolismo
Desoxirribonucleases de Sítio Específico do Tipo I/genética
Desoxirribonucleases de Sítio Específico do Tipo I/metabolismo
Recombinação Homóloga/genética
Simulação de Dinâmica Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA-Binding Proteins); EC 3.1.21.- (endodeoxyribonuclease I-Dmo I); EC 3.1.21.1 (Deoxyribonuclease I); EC 3.1.21.3 (Deoxyribonucleases, Type I Site-Specific)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150606
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.658666


  8 / 224 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26039067
[Au] Autor:Csefalvay E; Lapkouski M; Guzanova A; Csefalvay L; Baikova T; Shevelev I; Bialevich V; Shamayeva K; Janscak P; Kuta Smatanova I; Panjikar S; Carey J; Weiserova M; Ettrich R
[Ad] Endereço:Center for Nanobiology and Structural Biology, Institute of Microbiology and Global Change Research Center, Academy of Sciences of the Czech Republic, Zamek 136, CZ-373 33 Nove Hrady, Czech Republic.
[Ti] Título:Functional coupling of duplex translocation to DNA cleavage in a type I restriction enzyme.
[So] Source:PLoS One;10(6):e0128700, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Type I restriction-modification enzymes are multifunctional heteromeric complexes with DNA cleavage and ATP-dependent DNA translocation activities located on motor subunit HsdR. Functional coupling of DNA cleavage and translocation is a hallmark of the Type I restriction systems that is consistent with their proposed role in horizontal gene transfer. DNA cleavage occurs at nonspecific sites distant from the cognate recognition sequence, apparently triggered by stalled translocation. The X-ray crystal structure of the complete HsdR subunit from E. coli plasmid R124 suggested that the triggering mechanism involves interdomain contacts mediated by ATP. In the present work, in vivo and in vitro activity assays and crystal structures of three mutants of EcoR124I HsdR designed to probe this mechanism are reported. The results indicate that interdomain engagement via ATP is indeed responsible for signal transmission between the endonuclease and helicase domains of the motor subunit. A previously identified sequence motif that is shared by the RecB nucleases and some Type I endonucleases is implicated in signaling.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/química
Desoxirribonucleases de Sítio Específico do Tipo I/química
Proteínas de Escherichia coli/química
Escherichia coli/genética
Exodesoxirribonuclease V/química
Subunidades Proteicas/química
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Cristalografia por Raios X
Clivagem do DNA
DNA Bacteriano
Desoxirribonucleases de Sítio Específico do Tipo I/genética
Desoxirribonucleases de Sítio Específico do Tipo I/metabolismo
Escherichia coli/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Exodesoxirribonuclease V/genética
Exodesoxirribonuclease V/metabolismo
Expressão Gênica
Modelos Moleculares
Mutação
Conformação de Ácido Nucleico
Plasmídeos/química
Plasmídeos/metabolismo
Sinais Direcionadores de Proteínas
Estrutura Terciária de Proteína
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Escherichia coli Proteins); 0 (Protein Sorting Signals); 0 (Protein Subunits); 8L70Q75FXE (Adenosine Triphosphate); EC 3.1.11.5 (Exodeoxyribonuclease V); EC 3.1.11.5 (exodeoxyribonuclease V, E coli); EC 3.1.21.3 (Deoxyribonucleases, Type I Site-Specific); EC 3.1.21.3 (HsdR protein, E coli)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150604
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0128700


  9 / 224 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:25607609
[Au] Autor:Li Z; Robinson D; Hirst JD
[Ad] Endereço:School of Chemistry, University of Nottingham, Nottingham NG7 2RD, UK. jonathan.hirst@nottingham.ac.uk.
[Ti] Título:Vibronic structure in the far-UV electronic circular dichroism spectra of proteins.
[So] Source:Faraday Discuss;177:329-44, 2015.
[Is] ISSN:1359-6640
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The Franck-Condon effect is considered and the vibrational structure of the πnbπ* transition of the peptide backbone is incorporated into matrix method calculations of the electronic circular dichroism (CD) spectra of proteins in the far-ultraviolet. We employ the state-averaged CASPT2 method to calculate the ground and πnbπ* excited state geometries and frequencies of N-methylacetamide (NMA), which represents the peptide chromophore. The results of these calculations are used to incorporate vibronic levels of the excited states into the matrix method calculation. The CD spectra of a set of 49 proteins, comprising a range of structural types, are calculated to assess the influence of the vibrational structure. The calculated spectra of α-helical proteins are better resolved using the vibronic parameters and correlation between the experimental and the calculated intensity of less regular ß structure proteins improves over most wavelengths in the far-UV. No obvious improvement is observed in the calculated spectra of regular ß-sheet proteins. Our high-level ab initio calculations of the vibronic structure of the πnbπ* transition in NMA have provided some further insight into the physical origins of the nature of protein CD spectra in the far-UV.
[Mh] Termos MeSH primário: Acetamidas/química
Concanavalina A/química
Desoxirribonucleases de Sítio Específico do Tipo I/química
Elétrons
Mioglobina/química
Elastase Pancreática/química
[Mh] Termos MeSH secundário: Animais
Canavalia/química
Bovinos
Dicroísmo Circular
Modelos Químicos
Peptídeos/química
Estrutura Secundária de Proteína
Teoria Quântica
Soluções
Raios Ultravioleta
Vibração
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acetamides); 0 (Myoglobin); 0 (Peptides); 0 (Solutions); 11028-71-0 (Concanavalin A); EC 3.1.21.3 (Deoxyribonucleases, Type I Site-Specific); EC 3.4.21.36 (Pancreatic Elastase); V0T777481M (N-methylacetamide)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:150414
[Lr] Data última revisão:
150414
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150122
[St] Status:MEDLINE
[do] DOI:10.1039/c4fd00163j


  10 / 224 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:25451462
[Au] Autor:Zhang N; Shao L; Jiang Y; Gu Y; Li Q; Liu J; Jiang W; Yang S
[Ad] Endereço:Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China; Graduate University of the Chinese Academy of Sciences, Beijing 100049, China.
[Ti] Título:I-SceI-mediated scarless gene modification via allelic exchange in Clostridium.
[So] Source:J Microbiol Methods;108:49-60, 2015 Jan.
[Is] ISSN:1872-8359
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Although gene disruption in Clostridium spp. with the TargeTron technology is much more effective than single-crossover integration, it cannot achieve gene modification via allelic exchange. Here, we developed a targeted, nonpolar, scarless gene modification system based on the I-SceI endonuclease. First, a replicative plasmid containing homology arms on either side of the target sequence and I-SceI recognition sites was integrated into the Clostridium chromosome, resulting in single-crossover integrants containing a mutant allele. Second, the cells were transformed with plasmids containing the synthetic gene (sceC) encoding the I-SceI enzyme, resulting in double-stranded breaks at the I-SceI recognition sites, which stimulated homologous recombination and yielded double-crossover mutants. Application of the method was demonstrated by deleting two genes (adc and glcG) from C. acetobutylicum ATCC 824 and one gene (adc) from C. beijerinckii NCIMB 8052, and by introducing point mutations into xylR of C. beijerinckii NCIMB 8052. The double-crossover mutants displayed similar fermentation phenotypes to those constructed with the TargeTron technology.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Clostridium/genética
Desoxirribonucleases de Sítio Específico do Tipo I/metabolismo
Engenharia Genética/métodos
[Mh] Termos MeSH secundário: Alelos
Recombinação Homóloga
Mutação
Plasmídeos/genética
Plasmídeos/metabolismo
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 3.1.21.3 (Deoxyribonucleases, Type I Site-Specific)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:141220
[Lr] Data última revisão:
141220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141203
[St] Status:MEDLINE



página 1 de 23 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde