Base de dados : MEDLINE
Pesquisa : D08.811.277.040.013.500.032.099.500 [Categoria DeCS]
Referências encontradas : 1002 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 101 ir para página                         

  1 / 1002 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28449241
[Au] Autor:Knuppertz L; Osiewacz HD
[Ad] Endereço:Institute of Molecular Biosciences and Cluster of Excellence 'Macromolecular Complexes', Department of Biosciences, J. W. Goethe University, Frankfurt, Germany.
[Ti] Título:Autophagy compensates impaired energy metabolism in CLPXP-deficient Podospora anserina strains and extends healthspan.
[So] Source:Aging Cell;16(4):704-715, 2017 Aug.
[Is] ISSN:1474-9726
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The degradation of nonfunctional mitochondrial proteins is of fundamental relevance for maintenance of cellular homeostasis. The heteromeric CLPXP protein complex in the mitochondrial matrix is part of this process. In the fungal aging model Podospora anserina, ablation of CLPXP leads to an increase in healthy lifespan. Here, we report that this counterintuitive increase depends on a functional autophagy machinery. In PaClpXP mutants, autophagy is involved in energy conservation and the compensation of impairments in respiration. Strikingly, despite the impact on mitochondrial function, it is not mitophagy but general autophagy that is constitutively induced and required for longevity. In contrast, in another long-lived mutant ablated for the mitochondrial PaIAP protease, autophagy is neither induced nor required for lifespan extension. Our data provide novel mechanistic insights into the capacity of different forms of autophagy to compensate impairments of specific components of the complex mitochondrial quality control network and about the biological role of mitochondrial CLPXP in the control of cellular energy metabolism.
[Mh] Termos MeSH primário: Autofagia/genética
Endopeptidase Clp/genética
Proteínas Fúngicas/genética
Regulação Fúngica da Expressão Gênica
Mitocôndrias/enzimologia
Podospora/genética
[Mh] Termos MeSH secundário: Divisão Celular
Endopeptidase Clp/deficiência
Metabolismo Energético/genética
Proteínas Fúngicas/metabolismo
Viabilidade Microbiana
Mitocôndrias/genética
Mutação
Podospora/enzimologia
Podospora/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); EC 3.4.21.92 (Endopeptidase Clp)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171201
[Lr] Data última revisão:
171201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1111/acel.12600


  2 / 1002 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28937985
[Au] Autor:Llamas E; Pulido P; Rodriguez-Concepcion M
[Ad] Endereço:Centre for Research in Agricultural Genomics (CRAG) CSIC-IRTA-UAB-UB, Campus UAB Bellaterra, Barcelona, Spain.
[Ti] Título:Interference with plastome gene expression and Clp protease activity in Arabidopsis triggers a chloroplast unfolded protein response to restore protein homeostasis.
[So] Source:PLoS Genet;13(9):e1007022, 2017 Sep.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Disruption of protein homeostasis in chloroplasts impairs the correct functioning of essential metabolic pathways, including the methylerythritol 4-phosphate (MEP) pathway for the production of plastidial isoprenoids involved in photosynthesis and growth. We previously found that misfolded and aggregated forms of the first enzyme of the MEP pathway are degraded by the Clp protease with the involvement of Hsp70 and Hsp100/ClpC1 chaperones in Arabidopsis thaliana. By contrast, the combined unfolding and disaggregating actions of Hsp70 and Hsp100/ClpB3 chaperones allow solubilization and hence reactivation of the enzyme. The repair pathway is promoted when the levels of ClpB3 proteins increase upon reduction of Clp protease activity in mutants or wild-type plants treated with the chloroplast protein synthesis inhibitor lincomycin (LIN). Here we show that LIN treatment rapidly increases the levels of aggregated proteins in the chloroplast, unleashing a specific retrograde signaling pathway that up-regulates expression of ClpB3 and other nuclear genes encoding plastidial chaperones. As a consequence, folding capacity is increased to restore protein homeostasis. This sort of chloroplast unfolded protein response (cpUPR) mechanism appears to be mediated by the heat shock transcription factor HsfA2. Expression of HsfA2 and cpUPR-related target genes is independent of GUN1, a central integrator of retrograde signaling pathways. However, double mutants defective in both GUN1 and plastome gene expression (or Clp protease activity) are seedling lethal, confirming that the GUN1 protein is essential for protein homeostasis in chloroplasts.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/genética
Cloroplastos/genética
Proteínas de Ligação a DNA/genética
Proteínas de Choque Térmico/genética
Proteínas de Plantas/genética
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Arabidopsis/genética
Endopeptidase Clp/genética
Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Genoma de Planta
Proteínas de Choque Térmico HSP70/biossíntese
Proteínas de Choque Térmico HSP70/genética
Fatores de Transcrição de Choque Térmico
Lincomicina/farmacologia
Chaperonas Moleculares/genética
Fotossíntese/genética
Plantas Geneticamente Modificadas
Plântulas/genética
Transdução de Sinais
Resposta a Proteínas não Dobradas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (APG6 protein, Arabidopsis); 0 (Arabidopsis Proteins); 0 (DNA-Binding Proteins); 0 (GUN1 protein, Arabidopsis); 0 (HSFA2 protein, Arabidopsis); 0 (HSP70 Heat-Shock Proteins); 0 (Heat Shock Transcription Factors); 0 (Heat-Shock Proteins); 0 (Hsp100 protein, Arabidopsis); 0 (Molecular Chaperones); 0 (Plant Proteins); 0 (Transcription Factors); BOD072YW0F (Lincomycin); EC 3.4.21.92 (Endopeptidase Clp)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170923
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007022


  3 / 1002 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28760849
[Au] Autor:Gerth U; Krieger E; Zühlke D; Reder A; Völker U; Hecker M
[Ad] Endereço:Institute of Microbiology, Ernst-Moritz-Arndt-Universität Greifswald, Greifswald, Germany Ulf.Gerth@uni-greifswald.de.
[Ti] Título:Stability of Proteins Out of Service: the GapB Case of Bacillus subtilis.
[So] Source:J Bacteriol;199(20), 2017 Oct 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:possesses two glyceraldehyde-3-phosphate dehydrogenases with opposite roles, the glycolytic NAD-dependent GapA and the NADP-dependent GapB enzyme, which is exclusively required during gluconeogenesis but not active under conditions promoting glycolysis. We propose that proteins that are no longer needed will be recognized and proteolyzed by Clp proteases and thereby recycled. To test this postulation, we analyzed the stability of the glycolytic enzyme GapA and the gluconeogenetic enzyme GapB in the presence and absence of glucose. It turned out that GapA remained rather stable under both glycolytic and gluconeogenetic conditions. In contrast, the gluconeogenetic enzyme GapB was degraded after a shift from malate to glucose (i.e., from gluconeogenesis to glycolysis), displaying an estimated half-life of approximately 3 h. Comparative pulse-chase labeling and immunoprecipitation experiments of the wild-type strain and isogenic mutants identified the ATP-dependent ClpCP protease as the enzyme responsible for the degradation of GapB. However, arginine protein phosphorylation, which was recently described as a general tagging mechanism for protein degradation, did not seem to play a role in GapB proteolysis, because GapB was also degraded in a mutant, lacking arginine kinase, in the same manner as in the wild type. GapB, the NADP-dependent glyceraldehyde-3-phosphosphate dehydrogenase, is essential for under gluconeogenetic conditions. However, after a shift to glycolytic conditions, GapB loses its physiological function within the cell and becomes susceptible to degradation, in contrast to GapA, the glycolytic NAD-dependent glyceraldehyde-3-phosphate dehydrogenase, which remains stable under glycolytic and gluconeogenetic conditions. Subsequently, GapB is proteolyzed in a ClpCP-dependent manner. According to our data, the arginine kinase McsB is not involved as adaptor protein in this process. ClpCP appears to be in charge in the removal of inoperable enzymes in , which is a strictly regulated process in which the precise recognition mechanism(s) remains to be identified.
[Mh] Termos MeSH primário: Bacillus subtilis/enzimologia
Bacillus subtilis/metabolismo
Endopeptidase Clp/metabolismo
Gliceraldeído-3-Fosfato Desidrogenase (NADP+)(Fosforiladora)/metabolismo
Proteólise
[Mh] Termos MeSH secundário: Glucose/metabolismo
Glicólise
Imunoprecipitação
Marcação por Isótopo
Estabilidade Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.2.1.13 (Glyceraldehyde-3-Phosphate Dehydrogenase (NADP+)(Phosphorylating)); EC 3.4.21.92 (Endopeptidase Clp); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171015
[Lr] Data última revisão:
171015
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE


  4 / 1002 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28566324
[Au] Autor:Quirós PM; Prado MA; Zamboni N; D'Amico D; Williams RW; Finley D; Gygi SP; Auwerx J
[Ad] Endereço:Laboratory for Integrative and Systems Physiology, Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
[Ti] Título:Multi-omics analysis identifies ATF4 as a key regulator of the mitochondrial stress response in mammals.
[So] Source:J Cell Biol;216(7):2027-2045, 2017 Jul 03.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial stress activates a mitonuclear response to safeguard and repair mitochondrial function and to adapt cellular metabolism to stress. Using a multiomics approach in mammalian cells treated with four types of mitochondrial stressors, we identify activating transcription factor 4 (ATF4) as the main regulator of the stress response. Surprisingly, canonical mitochondrial unfolded protein response genes mediated by ATF5 are not activated. Instead, ATF4 activates the expression of cytoprotective genes, which reprogram cellular metabolism through activation of the integrated stress response (ISR). Mitochondrial stress promotes a local proteostatic response by reducing mitochondrial ribosomal proteins, inhibiting mitochondrial translation, and coupling the activation of the ISR with the attenuation of mitochondrial function. Through a trans-expression quantitative trait locus analysis, we provide genetic evidence supporting a role for Fh1 in the control of Atf4 expression in mammals. Using gene expression data from mice and humans with mitochondrial diseases, we show that the ATF4 pathway is activated in vivo upon mitochondrial stress. Our data illustrate the value of a multiomics approach to characterize complex cellular networks and provide a versatile resource to identify new regulators of mitochondrial-related diseases.
[Mh] Termos MeSH primário: Fator 4 Ativador da Transcrição/metabolismo
Metabolismo Energético
Genômica/métodos
Mitocôndrias/metabolismo
Doenças Mitocondriais/metabolismo
Proteínas Mitocondriais/metabolismo
Proteômica/métodos
Estresse Fisiológico
[Mh] Termos MeSH secundário: Fator 4 Ativador da Transcrição/genética
Animais
Biologia Computacional
Modelos Animais de Doenças
Endopeptidase Clp/genética
Endopeptidase Clp/metabolismo
Epigênese Genética
Regulação da Expressão Gênica
Redes Reguladoras de Genes
Predisposição Genética para Doença
Células HeLa
Serina Peptidase 2 de Requerimento de Alta Temperatura A
Seres Humanos
Potencial da Membrana Mitocondrial
Camundongos
Camundongos Knockout
Mitocôndrias/patologia
Doenças Mitocondriais/genética
Doenças Mitocondriais/patologia
Proteínas Mitocondriais/genética
Fenótipo
Complexo de Endopeptidases do Proteassoma/metabolismo
Mapas de Interação de Proteínas
Proteólise
Proteoma
Proteínas Ribossômicas/genética
Proteínas Ribossômicas/metabolismo
Serina Endopeptidases/genética
Serina Endopeptidases/metabolismo
Transdução de Sinais
Fatores de Tempo
Transcriptoma
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ATF4 protein, human); 0 (Atf4 protein, mouse); 0 (Mitochondrial Proteins); 0 (Proteome); 0 (Ribosomal Proteins); 145891-90-3 (Activating Transcription Factor 4); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.108 (High-Temperature Requirement A Serine Peptidase 2); EC 3.4.21.92 (CLPP protein, mouse); EC 3.4.21.92 (Endopeptidase Clp); EC 3.4.25.1 (Proteasome Endopeptidase Complex); EC 3.4.99.- (ATP dependent 26S protease)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170602
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201702058


  5 / 1002 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28507098
[Au] Autor:Joshi KK; Sutherland M; Chien P
[Ad] Endereço:From the Department of Biochemistry and Molecular Biology and.
[Ti] Título:Cargo engagement protects protease adaptors from degradation in a substrate-specific manner.
[So] Source:J Biol Chem;292(26):10973-10982, 2017 Jun 30.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein degradation in bacteria is a highly controlled process involving proteolytic adaptors that regulate protein degradation during cell cycle progression or during stress responses. Many adaptors work as scaffolds that selectively bind cargo and tether substrates to their cognate proteases to promote substrate destruction, whereas others primarily activate the target protease. Because adaptors must bind their cognate protease, all adaptors run the risk of being recognized by the protease as substrates themselves, a process that could limit their effectiveness. Here we use purified proteins in a reconstituted system and studies to show that adaptors of the ClpXP protease are readily degraded but that cargo binding inhibits this degradation. We found that this principle extends across several adaptor systems, including the hierarchical adaptors that drive the bacterial cell cycle and the quality control adaptor SspB. We also found that the ability of a cargo to protect its adaptor is adaptor substrate-specific, as adaptors with artificial degradation tags were not protected even though cargo binding is unaffected. Our work points to an optimization of inherent adaptor degradation and cargo binding that ensures that robust adaptor activity is maintained when high amounts of substrate must be delivered and that adaptors can be eliminated when their tasks have been completed.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Proteínas de Transporte/metabolismo
Caulobacter/enzimologia
Endopeptidase Clp/metabolismo
Proteólise
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Transporte/genética
Caulobacter/genética
Endopeptidase Clp/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Carrier Proteins); EC 3.4.21.92 (Endopeptidase Clp)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170715
[Lr] Data última revisão:
170715
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170517
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.786392


  6 / 1002 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28431231
[Au] Autor:Yeom J; Wayne KJ; Groisman EA
[Ad] Endereço:Department of Microbial Pathogenesis, Yale School of Medicine, 295 Congress Avenue, New Haven, CT 06536, USA.
[Ti] Título:Sequestration from Protease Adaptor Confers Differential Stability to Protease Substrate.
[So] Source:Mol Cell;66(2):234-246.e5, 2017 Apr 20.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:According to the N-end rule, the N-terminal residue of a protein determines its stability. In bacteria, the adaptor ClpS mediates proteolysis by delivering substrates bearing specific N-terminal residues to the protease ClpAP. We now report that the Salmonella adaptor ClpS binds to the N terminus of the regulatory protein PhoP, resulting in PhoP degradation by ClpAP. We establish that the PhoP-activated protein MgtC protects PhoP from degradation by outcompeting ClpS for binding to PhoP. MgtC appears to act exclusively on PhoP, as it did not alter the stability of a different ClpS-dependent ClpAP substrate. Removal of five N-terminal residues rendered PhoP stability independent of both the clpS and mgtC genes. By preserving PhoP protein levels, MgtC enables normal temporal transcription of PhoP-activated genes. The identified mechanism provides a simple means to spare specific substrates from an adaptor-dependent protease.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Proteínas de Transporte de Cátions/metabolismo
Endopeptidase Clp/metabolismo
Salmonella typhimurium/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Ligação Competitiva
Proteínas de Transporte de Cátions/química
Proteínas de Transporte de Cátions/genética
Endopeptidase Clp/química
Endopeptidase Clp/genética
Regulação Bacteriana da Expressão Gênica
Meia-Vida
Modelos Moleculares
Mutação
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estabilidade Proteica
Proteólise
Salmonella typhimurium/genética
Relação Estrutura-Atividade
Especificidade por Substrato
Fatores de Tempo
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cation Transport Proteins); 125360-99-8 (PhoP protein, Bacteria); EC 3.4.21.92 (Endopeptidase Clp); EC 3.6.1.- (MgtC protein, Salmonella typhimurium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170908
[Lr] Data última revisão:
170908
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170422
[St] Status:MEDLINE


  7 / 1002 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28375422
[Au] Autor:Malik IT; Brötz-Oesterhelt H
[Ad] Endereço:Department of Microbial Bioactive Compounds, Interfaculty Institute of Microbiology and Infection Medicine, University of Tuebingen, Germany. heike.broetz-oesterhelt@uni-tuebingen.de.
[Ti] Título:Conformational control of the bacterial Clp protease by natural product antibiotics.
[So] Source:Nat Prod Rep;34(7):815-831, 2017 Jul 06.
[Is] ISSN:1460-4752
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Covering: up to 2017The bacterial Clp protease is a highly conserved and structurally versatile machine. It has gained a lot of recognition during the last decade as a novel antibacterial drug target with an unprecedented mechanism of action. Due to its complexity, there are distinct means of interfering with its natural functions and several compounds targeting this machine have been identified. In this review, we summarize the current state of knowledge about natural products deregulating Clp proteolysis, a crucial and delicate process within the cell. Among those, acyldepsipeptide antibiotics of the ADEP class (ADEPs) are characterized best. The molecular mechanism of ADEP-mediated deregulation sheds light on the inner workings of the Clp protease.
[Mh] Termos MeSH primário: Antibacterianos/química
Proteínas de Bactérias/química
Produtos Biológicos/química
Endopeptidase Clp/metabolismo
[Mh] Termos MeSH secundário: Depsipeptídeos/química
Estrutura Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Biological Products); 0 (Depsipeptides); EC 3.4.21.92 (Endopeptidase Clp)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170809
[Lr] Data última revisão:
170809
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170405
[St] Status:MEDLINE
[do] DOI:10.1039/c6np00125d


  8 / 1002 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28335002
[Au] Autor:Bury K; Wegrzyn K; Konieczny I
[Ad] Endereço:Department of Molecular and Cellular Biology, Intercollegiate Faculty of Biotechnology of University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-308 Gdansk, Poland.
[Ti] Título:Handcuffing reversal is facilitated by proteases and replication initiator monomers.
[So] Source:Nucleic Acids Res;45(7):3953-3966, 2017 Apr 20.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Specific nucleoprotein complexes are formed strictly to prevent over-initiation of DNA replication. An example of those is the so-called handcuff complex, in which two plasmid molecules are coupled together with plasmid-encoded replication initiation protein (Rep). In this work, we elucidate the mechanism of the handcuff complex disruption. In vitro tests, including dissociation progress analysis, demonstrate that the dimeric variants of plasmid RK2 replication initiation protein TrfA are involved in assembling the plasmid handcuff complex which, as we found, reveals high stability. Particular proteases, namely Lon and ClpAP, disrupt the handcuff by degrading TrfA, thus affecting plasmid stability. Moreover, our data demonstrate that TrfA monomers are able to dissociate handcuffed plasmid molecules. Those monomers displace TrfA molecules, which are involved in handcuff formation, and through interaction with the uncoupled plasmid replication origins they re-initiate DNA synthesis. We discuss the relevance of both Rep monomers and host proteases for plasmid maintenance under vegetative and stress conditions.
[Mh] Termos MeSH primário: Replicação do DNA
Endopeptidase Clp/metabolismo
Proteínas de Escherichia coli/metabolismo
Plasmídeos/biossíntese
Protease La/metabolismo
[Mh] Termos MeSH secundário: DNA Bacteriano/biossíntese
Escherichia coli/enzimologia
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas de Escherichia coli/genética
Nucleoproteínas/metabolismo
Plasmídeos/metabolismo
Protease La/genética
Multimerização Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Escherichia coli Proteins); 0 (Nucleoproteins); 0 (TrfA protein, E coli); EC 3.4.21.53 (ClpA protease, E coli); EC 3.4.21.53 (Lon protein, E coli); EC 3.4.21.53 (Protease La); EC 3.4.21.92 (ClpP protease, E coli); EC 3.4.21.92 (Endopeptidase Clp)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx166


  9 / 1002 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28228329
[Au] Autor:Wurm P; Tutz S; Mutsam B; Vorkapic D; Heyne B; Grabner C; Kleewein K; Halscheidt A; Schild S; Reidl J
[Ad] Endereço:University of Graz, Institute of Molecular Biosciences, Molecular Enzymology and Physiology, Humboldtstraße 50, A-8010 Graz, Austria.
[Ti] Título:Stringent factor and proteolysis control of sigma factor RpoS expression in Vibrio cholerae.
[So] Source:Int J Med Microbiol;307(3):154-165, 2017 Apr.
[Is] ISSN:1618-0607
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Vibrio cholerae can colonize the gastrointestinal track of humans and cause the disease cholera. During colonization, the alternative sigma factor, RpoS, controls a process known as "mucosal escape response," defining a specific spatial and temporal response and effecting chemotaxis and motility. In this report, the expression and proteolytic control of RpoS in V. cholerae was characterized. To date, aspects of proteolysis control, the involved components, and proteolysis regulation have not been addressed for RpoS in V. cholerae. Similar to Escherichia coli, we find that the RpoS protein is subjected to regulated intracellular proteolysis, which is mediated by homologues of the proteolysis-targeting factor RssB and the protease complex ClpXP. As demonstrated, RpoS expression transiently peaks after cells are shifted from rich to minimal growth medium. This peak level is dependent on (p)ppGpp-activated rpoS transcription and controlled RpoS proteolysis. The RpoS peak level also correlates with induction of a chemotaxis gene, encoding a methyl-accepting chemotaxis protein, earlier identified to belong to the mucosal escape response pathway. These results suggest that the RpoS expression peak is linked to (p)ppGpp alarmone increase, leading to enhanced motility and chemotaxis, and possibly contributing to the mucosal escape response.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Endopeptidase Clp/metabolismo
GTP Pirofosfoquinase/metabolismo
Regulação Bacteriana da Expressão Gênica
Fator sigma/metabolismo
Vibrio cholerae/genética
Vibrio cholerae/metabolismo
[Mh] Termos MeSH secundário: Quimiotaxia
Meios de Cultura/química
Seres Humanos
Proteólise
Vibrio cholerae/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Culture Media); 0 (Sigma Factor); 0 (sigma factor KatF protein, Bacteria); EC 2.7.6.5 (GTP Pyrophosphokinase); EC 3.4.21.92 (Endopeptidase Clp)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170224
[St] Status:MEDLINE


  10 / 1002 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28223361
[Au] Autor:Baytshtok V; Chen J; Glynn SE; Nager AR; Grant RA; Baker TA; Sauer RT
[Ad] Endereço:From the Department of Biology and.
[Ti] Título:Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation.
[So] Source:J Biol Chem;292(14):5695-5704, 2017 Apr 07.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The HslUV proteolytic machine consists of HslV, a double-ring self-compartmentalized peptidase, and one or two AAA+ HslU ring hexamers that hydrolyze ATP to power the unfolding of protein substrates and their translocation into the proteolytic chamber of HslV. Here, we use genetic tethering and disulfide bonding strategies to construct HslU pseudohexamers containing mixtures of ATPase active and inactive subunits at defined positions in the hexameric ring. Genetic tethering impairs HslV binding and degradation, even for pseudohexamers with six active subunits, but disulfide-linked pseudohexamers do not have these defects, indicating that the peptide tether interferes with HslV interactions. Importantly, pseudohexamers containing different patterns of hydrolytically active and inactive subunits retain the ability to unfold protein substrates and/or collaborate with HslV in their degradation, supporting a model in which ATP hydrolysis and linked mechanical function in the HslU ring operate by a probabilistic mechanism.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/química
Endopeptidase Clp/química
Proteínas de Escherichia coli/química
Escherichia coli/enzimologia
Desdobramento de Proteína
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/genética
Trifosfato de Adenosina/metabolismo
Domínio Catalítico
Endopeptidase Clp/genética
Endopeptidase Clp/metabolismo
Escherichia coli/genética
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ClpYQ protease, E coli); 0 (Escherichia coli Proteins); 8L70Q75FXE (Adenosine Triphosphate); EC 3.4.21.92 (Endopeptidase Clp)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170223
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.768978



página 1 de 101 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