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  1 / 389 MEDLINE  
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[PMID]:26755601
[Au] Autor:Holm M; Borg A; Ehrenberg M; Sanyal S
[Ad] Endereço:Department of Cell and Molecular biology, Uppsala University, 75124 Uppsala, Sweden.
[Ti] Título:Molecular mechanism of viomycin inhibition of peptide elongation in bacteria.
[So] Source:Proc Natl Acad Sci U S A;113(4):978-83, 2016 Jan 26.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Viomycin is a tuberactinomycin antibiotic essential for treating multidrug-resistant tuberculosis. It inhibits bacterial protein synthesis by blocking elongation factor G (EF-G) catalyzed translocation of messenger RNA on the ribosome. Here we have clarified the molecular aspects of viomycin inhibition of the elongating ribosome using pre-steady-state kinetics. We found that the probability of ribosome inhibition by viomycin depends on competition between viomycin and EF-G for binding to the pretranslocation ribosome, and that stable viomycin binding requires an A-site bound tRNA. Once bound, viomycin stalls the ribosome in a pretranslocation state for a minimum of ∼ 45 s. This stalling time increases linearly with viomycin concentration. Viomycin inhibition also promotes futile cycles of GTP hydrolysis by EF-G. Finally, we have constructed a kinetic model for viomycin inhibition of EF-G catalyzed translocation, allowing for testable predictions of tuberactinomycin action in vivo and facilitating in-depth understanding of resistance development against this important class of antibiotics.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Bactérias/efeitos dos fármacos
Fator G para Elongação de Peptídeos/antagonistas & inibidores
Biossíntese de Proteínas/efeitos dos fármacos
Viomicina/farmacologia
[Mh] Termos MeSH secundário: Bactérias/metabolismo
Relação Dose-Resposta a Droga
Guanosina Trifosfato/química
Probabilidade
Ribossomos/efeitos dos fármacos
Ribossomos/metabolismo
Viomicina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Peptide Elongation Factor G); 86-01-1 (Guanosine Triphosphate); YVU35998K5 (Viomycin)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160113
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1517541113


  2 / 389 MEDLINE  
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[PMID]:26554029
[Au] Autor:Zeng F; Jin H
[Ad] Endereço:Department of Biochemistry, Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
[Ti] Título:Peptide release promoted by methylated RF2 and ArfA in nonstop translation is achieved by an induced-fit mechanism.
[So] Source:RNA;22(1):49-60, 2016 Jan.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Here we report that the specificity of peptide release in the ribosome on a nonstop mRNA by ArfA and RF2 is achieved by an induced-fit mechanism. Using RF2 that is methylated on the glutamine of its GGQ motif (RF2(m)), we show that methylation substantially increases the rate of ArfA/RF2-catalyzed peptide release on a nonstop mRNA that does not occupy the ribosomal A site, but has only a modest effect on k(cat) by the same proteins on longer nonstop mRNAs occupying the A site of the mRNA channel in the ribosome. Our data suggest that enhancement in the kcat of peptide release by ArfA and RF2 under the cognate decoding condition is the result of favorable conformational changes in the nonstop complex. We demonstrate a shared mechanism between canonical and nonstop termination, supported by similarities in the kinetic mechanisms in antibiotic inhibition and methylation-correlated enhancement in the rate of peptide release. Despite these similarities, our data suggest that nonstop termination differs from canonical pathway in the downstream event of recycling.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/metabolismo
Fatores de Terminação de Peptídeos/metabolismo
Peptídeos/metabolismo
Biossíntese de Proteínas
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Biocatálise
Escherichia coli/metabolismo
Metilação
Paromomicina/farmacologia
Terminação Traducional da Cadeia Peptídica
Ribossomos/metabolismo
Viomicina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ArfA protein, E coli); 0 (Escherichia coli Proteins); 0 (Peptide Termination Factors); 0 (Peptides); 0 (RNA-Binding Proteins); 0 (prfB protein, E coli); 61JJC8N5ZK (Paromomycin); YVU35998K5 (Viomycin)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:170101
[Lr] Data última revisão:
170101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151111
[St] Status:MEDLINE
[do] DOI:10.1261/rna.053082.115


  3 / 389 MEDLINE  
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[PMID]:25288752
[Au] Autor:Salsi E; Farah E; Dann J; Ermolenko DN
[Ad] Endereço:Department of Biochemistry and Biophysics and Center for RNA Biology, School of Medicine and Dentistry, University of Rochester, Rochester, NY 14642.
[Ti] Título:Following movement of domain IV of elongation factor G during ribosomal translocation.
[So] Source:Proc Natl Acad Sci U S A;111(42):15060-5, 2014 Oct 21.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Translocation of mRNA and tRNAs through the ribosome is catalyzed by a universally conserved elongation factor (EF-G in prokaryotes and EF-2 in eukaryotes). Previous studies have suggested that ribosome-bound EF-G undergoes significant structural rearrangements. Here, we follow the movement of domain IV of EF-G, which is critical for the catalysis of translocation, relative to protein S12 of the small ribosomal subunit using single-molecule FRET. We show that ribosome-bound EF-G adopts distinct conformations corresponding to the pre- and posttranslocation states of the ribosome. Our results suggest that, upon ribosomal translocation, domain IV of EF-G moves toward the A site of the small ribosomal subunit and facilitates the movement of peptidyl-tRNA from the A to the P site. We found no evidence of direct coupling between the observed movement of domain IV of EF-G and GTP hydrolysis. In addition, our results suggest that the pretranslocation conformation of the EF-G-ribosome complex is significantly less stable than the posttranslocation conformation. Hence, the structural rearrangement of EF-G makes a considerable energetic contribution to promoting tRNA translocation.
[Mh] Termos MeSH primário: Fator G para Elongação de Peptídeos/metabolismo
Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Transporte Biológico
Catálise
Transferência Ressonante de Energia de Fluorescência
Guanosina Trifosfato/química
Microscopia
Ligação Proteica
Estrutura Terciária de Proteína
Inibidores da Síntese de Proteínas/química
Transporte Proteico
RNA Mensageiro/metabolismo
RNA de Transferência/química
Ribossomos/química
Viomicina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Peptide Elongation Factor G); 0 (Protein Synthesis Inhibitors); 0 (RNA, Messenger); 86-01-1 (Guanosine Triphosphate); 9014-25-9 (RNA, Transfer); YVU35998K5 (Viomycin)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141008
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1410873111


  4 / 389 MEDLINE  
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[PMID]:25205267
[Au] Autor:Iscla I; Wray R; Wei S; Posner B; Blount P
[Ad] Endereço:Department of Physiology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-9040, USA.
[Ti] Título:Streptomycin potency is dependent on MscL channel expression.
[So] Source:Nat Commun;5:4891, 2014 Sep 10.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The antibiotic streptomycin is widely used in the treatment of microbial infections. The primary mechanism of action is inhibition of translation by binding to the ribosome, but how it enters the bacterial cell is unclear. Early in the study of this antibiotic, a mysterious streptomycin-induced potassium efflux preceding any decrease in viability was observed; it was speculated that this changed the electrochemical gradient such that streptomycin better accessed the cytoplasm. Here we use a high-throughput screen to search for compounds targeting the mechanosensitive channel of large conductance (MscL) and find dihydrostreptomycin among the 'hits'. Furthermore, we find that MscL is not only necessary for the previously described streptomycin-induced potassium efflux, but also directly increases MscL activity in electrophysiological studies. The data suggest that gating MscL is a novel mode of action of dihydrostreptomycin, and that MscL's large pore may provide a mechanism for cell entry.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Sulfato de Di-Hidroestreptomicina/farmacologia
Proteínas de Escherichia coli/efeitos dos fármacos
Escherichia coli/efeitos dos fármacos
Canais Iônicos/efeitos dos fármacos
Potássio/metabolismo
[Mh] Termos MeSH secundário: Sulfato de Di-Hidroestreptomicina/metabolismo
Escherichia coli/metabolismo
Proteínas de Escherichia coli/metabolismo
Ensaios de Triagem em Larga Escala
Canais Iônicos/metabolismo
Técnicas de Patch-Clamp
Espectinomicina/farmacologia
Estreptomicina/metabolismo
Estreptomicina/farmacologia
Viomicina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Escherichia coli Proteins); 0 (Ion Channels); 0 (MscL protein, E coli); 93AKI1U6QF (Spectinomycin); RWP5GA015D (Potassium); T7D4876IUE (Dihydrostreptomycin Sulfate); Y45QSO73OB (Streptomycin); YVU35998K5 (Viomycin)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140911
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms5891


  5 / 389 MEDLINE  
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[PMID]:23545648
[Au] Autor:Bloudoff K; Schmeing TM
[Ad] Endereço:Department of Biochemistry, McGill University, Montréal, QC H3G 0B1, Canada.
[Ti] Título:Crystallization and preliminary crystallographic analysis of the first condensation domain of viomycin synthetase.
[So] Source:Acta Crystallogr Sect F Struct Biol Cryst Commun;69(Pt 4):412-5, 2013 Apr 01.
[Is] ISSN:1744-3091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Nonribosomal peptide synthetases (NRPSs) are large multimodular enzymes that synthesize important secondary metabolites such as antibiotics. NRPSs follow a modular synthetic logic whereby each successive amino-acid monomer is added to the peptide chain by successive multi-domain modules. The condensation domain catalyzes the central chemical event in the synthetic cycle, peptide-bond formation, and is present in every elongation module of the NRPS. Viomycin is an antituberculosis nonribosomal peptide that is synthesized by a series of four NRPS proteins and then modified by tailoring proteins. In order to study the mechanisms of peptide-bond formation in viomycin and in NRPSs in general, a structural study of the first condensation domain of the viomycin synthetase protein VioA (VioA-C1) was initiated. The gene for VioA-C1 was cloned from genomic DNA of Streptomyces vinaceus, expressed as an octahistidine-tagged construct and purified by column chromatography. VioA-C1 was crystallized using the sitting-drop vapor-diffusion method. X-ray diffraction data were collected on a rotating-anode source to 2.9 Å resolution. The data could be indexed in the orthorhombic space group P212121, with unit-cell parameters a = 46.165, b = 68.335, c = 146.423 Å. There is likely to be one monomer in the asymmetric unit, giving a solvent content of 49.2% and a Matthews coefficient (VM) of 2.42 Å(3) Da(-1). Structural determination is in progress.
[Mh] Termos MeSH primário: Peptídeo Sintases/química
Streptomyces/enzimologia
[Mh] Termos MeSH secundário: Cristalização
Cristalografia por Raios X
Peptídeo Sintases/metabolismo
Viomicina/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 6.3.2.- (Peptide Synthases); YVU35998K5 (Viomycin)
[Em] Mês de entrada:1312
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130403
[St] Status:MEDLINE
[do] DOI:10.1107/S1744309113004004


  6 / 389 MEDLINE  
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[PMID]:22779429
[Au] Autor:Monshupanee T; Johansen SK; Dahlberg AE; Douthwaite S
[Ad] Endereço:Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark. tanakarn.m@chula.ac.th
[Ti] Título:Capreomycin susceptibility is increased by TlyA-directed 2'-O-methylation on both ribosomal subunits.
[So] Source:Mol Microbiol;85(6):1194-203, 2012 Sep.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The binding site of the cyclic peptide antibiotics capreomycin and viomycin is located on the ribosomal subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA. In Mycobacterium tuberculosis, the 2'-hydroxyls of both nucleotides are methylated by the enzyme TlyA. Loss of these methylations through inactivation of TlyA confers resistance to capreomycin and viomycin. We report here that TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, now termed TlyA(I) , has shorter N- and C-termini and methylates only C1920; the second group (now TlyA(II) ) includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 and C1920. Ribosomal subunits are the preferred substrates for both groups of orthologues. Amino acid substitutions at the N-terminus of TlyA(II) reduce its ability to methylate these substrates. Growing pairs of recombinant TlyA(II) Escherichia coli strains in competition shows that even subtle changes in the level of rRNA methylation lead to significant differences in susceptibility to sub-inhibitory concentrations of capreomycin. The findings reveal that 2'-O-methyls at both C1409 and C1920 play a role in facilitating the inhibitory effects of capreomycin and viomycin on the bacterial ribosome.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Bactérias/efeitos dos fármacos
Bactérias/enzimologia
Proteínas de Bactérias/metabolismo
Capreomicina/farmacologia
RNA Ribossômico/metabolismo
tRNA Metiltransferases/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Metilação
Testes de Sensibilidade Microbiana
Modelos Moleculares
Conformação de Ácido Nucleico
Subunidades Ribossômicas/metabolismo
Viomicina/farmacologia
tRNA Metiltransferases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (RNA, Ribosomal); 11003-38-6 (Capreomycin); EC 2.1.1.- (tRNA Methyltransferases); YVU35998K5 (Viomycin)
[Em] Mês de entrada:1301
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120712
[St] Status:MEDLINE
[do] DOI:10.1111/j.1365-2958.2012.08168.x


  7 / 389 MEDLINE  
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[PMID]:22187675
[Au] Autor:Zhou J; Lancaster L; Trakhanov S; Noller HF
[Ad] Endereço:Center for Molecular Biology of RNA and Department of Molecular, Cell and Developmental Biology, University of California at Santa Cruz, CA 95064, USA.
[Ti] Título:Crystal structure of release factor RF3 trapped in the GTP state on a rotated conformation of the ribosome.
[So] Source:RNA;18(2):230-40, 2012 Feb.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The class II release factor RF3 is a GTPase related to elongation factor EF-G, which catalyzes release of class I release factors RF1 and RF2 from the ribosome after termination of protein synthesis. The 3.3 Å crystal structure of the RF3·GDPNP·ribosome complex provides a high-resolution description of interactions and structural rearrangements that occur when binding of this translational GTPase induces large-scale rotational movements in the ribosome. RF3 induces a 7° rotation of the body and 14° rotation of the head of the 30S ribosomal subunit, and itself undergoes inter- and intradomain conformational rearrangements. We suggest that ordering of critical elements of switch loop I and the P loop, which help to form the GTPase catalytic site, are caused by interactions between the G domain of RF3 and the sarcin-ricin loop of 23S rRNA. The rotational movements in the ribosome induced by RF3, and its distinctly different binding orientation to the sarcin-ricin loop of 23S rRNA, raise interesting implications for the mechanism of action of EF-G in translocation.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/química
Guanosina Trifosfato/química
Fatores de Terminação de Peptídeos/química
Ribossomos/química
[Mh] Termos MeSH secundário: Domínio Catalítico
Cristalografia por Raios X
Escherichia coli/metabolismo
Proteínas de Escherichia coli/metabolismo
GTP Fosfo-Hidrolases/química
GTP Fosfo-Hidrolases/metabolismo
Guanosina Trifosfato/metabolismo
Modelos Moleculares
Fator G para Elongação de Peptídeos/metabolismo
Fatores de Terminação de Peptídeos/metabolismo
Ligação Proteica/efeitos dos fármacos
Biossíntese de Proteínas/efeitos dos fármacos
Estrutura Terciária de Proteína/efeitos dos fármacos
RNA Ribossômico 23S/metabolismo
Ribossomos/metabolismo
Translocação Genética/efeitos dos fármacos
Translocação Genética/genética
Viomicina/farmacologia
[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 (Escherichia coli Proteins); 0 (Peptide Elongation Factor G); 0 (Peptide Termination Factors); 0 (RNA, Ribosomal, 23S); 0 (prfC protein, E coli); 86-01-1 (Guanosine Triphosphate); EC 3.6.1.- (GTP Phosphohydrolases); YVU35998K5 (Viomycin)
[Em] Mês de entrada:1205
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:111222
[St] Status:MEDLINE
[do] DOI:10.1261/rna.031187.111


  8 / 389 MEDLINE  
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[PMID]:21768509
[Au] Autor:Akbergenov R; Shcherbakov D; Matt T; Duscha S; Meyer M; Wilson DN; Böttger EC
[Ad] Endereço:Institut für Medizinische Mikrobiologie, Universität Zürich, Gloriastrasse 30/32, 8006 Zürich, Switzerland.
[Ti] Título:Molecular basis for the selectivity of antituberculosis compounds capreomycin and viomycin.
[So] Source:Antimicrob Agents Chemother;55(10):4712-7, 2011 Oct.
[Is] ISSN:1098-6596
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Capreomycin and the structurally similar compound viomycin are cyclic peptide antibiotics which are particularly active against Mycobacterium tuberculosis, including multidrug resistant strains. Both antibiotics bind across the ribosomal interface involving 23S rRNA helix 69 (H69) and 16S rRNA helix 44 (h44). The binding site of tuberactinomycins in h44 partially overlaps with that of aminoglycosides, and they share with these drugs the side effect of irreversible hearing loss. Here we studied the drug target interaction on ribosomes modified by site-directed mutagenesis. We identified rRNA residues in h44 as the main determinants of phylogenetic selectivity, predict compensatory evolution to impact future resistance development, and propose mechanisms involved in tuberactinomycin ototoxicity, which may enable the development of improved, less-toxic derivatives.
[Mh] Termos MeSH primário: Antituberculosos/farmacologia
Capreomicina/farmacologia
Mycobacterium tuberculosis/efeitos dos fármacos
Ribossomos/efeitos dos fármacos
Viomicina/farmacologia
[Mh] Termos MeSH secundário: Aminoglicosídeos/farmacologia
Antituberculosos/metabolismo
Antituberculosos/toxicidade
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Capreomicina/metabolismo
Capreomicina/toxicidade
Farmacorresistência Bacteriana Múltipla/genética
Enviomicina/análogos & derivados
Enviomicina/farmacologia
Enviomicina/toxicidade
Mutagênese Sítio-Dirigida
Mycobacterium tuberculosis/genética
Mycobacterium tuberculosis/metabolismo
RNA Ribossômico 16S/metabolismo
RNA Ribossômico 23S/metabolismo
Viomicina/metabolismo
Viomicina/toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Aminoglycosides); 0 (Antitubercular Agents); 0 (Bacterial Proteins); 0 (RNA, Ribosomal, 16S); 0 (RNA, Ribosomal, 23S); 11003-38-6 (Capreomycin); 85B3A97YJY (tuberactinomycin); XU299C23A2 (Enviomycin); YVU35998K5 (Viomycin)
[Em] Mês de entrada:1203
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110720
[St] Status:MEDLINE
[do] DOI:10.1128/AAC.00628-11


  9 / 389 MEDLINE  
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[PMID]:21739558
[Au] Autor:Felnagle EA; Podevels AM; Barkei JJ; Thomas MG
[Ad] Endereço:Department of Bacteriology, University of Wisconsin-Madison, Madison, WI 53706, USA.
[Ti] Título:Mechanistically distinct nonribosomal peptide synthetases assemble the structurally related antibiotics viomycin and capreomycin.
[So] Source:Chembiochem;12(12):1859-67, 2011 Aug 16.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Mh] Termos MeSH primário: Antituberculosos/metabolismo
Proteínas de Bactérias/química
Capreomicina/metabolismo
Engenharia Metabólica/métodos
Biossíntese de Peptídeos Independentes de Ácido Nucleico/genética
Peptídeo Sintases/química
Proteínas Recombinantes/química
Viomicina/metabolismo
[Mh] Termos MeSH secundário: Antituberculosos/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Capreomicina/química
Cromatografia Líquida de Alta Pressão
Primers do DNA
Escherichia coli/enzimologia
Escherichia coli/genética
Tuberculose Extensivamente Resistente a Medicamentos/tratamento farmacológico
Tuberculose Extensivamente Resistente a Medicamentos/microbiologia
Mycobacterium tuberculosis/efeitos dos fármacos
Mycobacterium tuberculosis/crescimento & desenvolvimento
Peptídeo Sintases/genética
Peptídeo Sintases/metabolismo
Plasmídeos
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Streptomyces lividans/enzimologia
Streptomyces lividans/genética
Homologia Estrutural de Proteína
Transformação Genética
Viomicina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Antitubercular Agents); 0 (Bacterial Proteins); 0 (DNA Primers); 0 (Recombinant Proteins); 11003-38-6 (Capreomycin); EC 6.3.2.- (Peptide Synthases); YVU35998K5 (Viomycin)
[Em] Mês de entrada:1112
[Cu] Atualização por classe:161025
[Lr] Data última revisão:
161025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110709
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201100193


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[PMID]:20886842
[Au] Autor:Ly CT; Altuntop ME; Wang Y
[Ad] Endereço:Department of Biology and Biochemistry, University of Houston, 4800 Calhoun Road, Houston, Texas 77214, United States.
[Ti] Título:Single-molecule study of viomycin's inhibition mechanism on ribosome translocation.
[So] Source:Biochemistry;49(45):9732-8, 2010 Nov 16.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Viomycin belongs to the tuberactinomycin family of antibiotics against tuberculosis. However, its inhibition mechanism remains elusive. Although it is clear that viomycin inhibits the ribosome intersubunit ratcheting, there are contradictory reports about whether the antibiotic viomycin stabilizes the tRNA hybrid or classical state. By using a single-molecule FRET method to directly observe the tRNA dynamics relative to ribosomal protein L27, we have found that viomycin trapped the hybrid state within certain ribosome subgroups but did not significantly suppress the tRNA dynamics. The persistent fluctuation of tRNA implied that tRNA motions were decoupled from the ribosome intersubunit ratcheting. Viomycin also promoted peptidyl-tRNA fluctuation in the posttranslocation complex, implying that, in addition to acylated P-site tRNA, the decoding center also played an important role of ribosome locking after translocation. Therefore, viomycin inhibits translocation by trapping the hybrid state in the pretranslocation complex and disturbing the stability of posttranslocation complex. Our results imply that ribosome translocation is possibly a synergistic process of multiple decoupled local dynamics.
[Mh] Termos MeSH primário: Ribossomos/efeitos dos fármacos
Viomicina/farmacologia
[Mh] Termos MeSH secundário: Transporte Biológico/efeitos dos fármacos
Transferência Ressonante de Energia de Fluorescência/métodos
Oligopeptídeos/biossíntese
Oligopeptídeos/metabolismo
Fator G para Elongação de Peptídeos/genética
Fator G para Elongação de Peptídeos/metabolismo
Biossíntese de Proteínas/efeitos dos fármacos
Transporte Proteico
RNA Mensageiro/genética
RNA de Transferência/efeitos dos fármacos
RNA de Transferência/genética
Ribossomos/genética
Ribossomos/metabolismo
Translocação Genética/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Oligopeptides); 0 (Peptide Elongation Factor G); 0 (RNA, Messenger); 9014-25-9 (RNA, Transfer); YVU35998K5 (Viomycin)
[Em] Mês de entrada:1012
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:101005
[St] Status:MEDLINE
[do] DOI:10.1021/bi101029g



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