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[PMID]:29331375
[Au] Autor:Ma L; Wang Q; Yuan M; Zou T; Yin P; Wang S
[Ad] Endereço:National Key Laboratory of Crop Genetic Improvement, National Center of Plant Gene Research (Wuhan), Huazhong Agricultural University, Wuhan 430070, China.
[Ti] Título:Xanthomonas TAL effectors hijack host basal transcription factor IIA α and γ subunits for invasion.
[So] Source:Biochem Biophys Res Commun;496(2):608-613, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Xanthomonas genus includes Gram-negative plant-pathogenic bacteria, which infect a broad range of crops and wild plant species, cause symptoms with leaf blights, streaks, spots, stripes, necrosis, wilt, cankers and gummosis on leaves, stems and fruits in a wide variety of plants via injecting their effector proteins into the host cell during infection. Among these virulent effectors, transcription activator-like effectors (TALEs) interact with the γ subunit of host transcription factor IIA (TFIIAγ) to activate the transcription of host disease susceptibility genes. Functional TFIIA is a ternary complex comprising α, ß and γ subunits. However, whether TALEs recruit TFIIAα, TFIIAß, or both remains unknown. The underlying molecular mechanisms by which TALEs mediate host susceptibility gene activation require full elucidation. Here, we show that TALEs interact with the α+γ binary subcomplex but not the α+ß+γ ternary complex of rice TFIIA (holo-OsTFIIA). The transcription factor binding (TFB) regions of TALEs, which are highly conserved in Xanthomonas species, have a dominant role in these interactions. Furthermore, the interaction between TALEs and the α+γ complex exhibits robust DNA binding activity in vitro. These results collectively demonstrate that TALE-carrying pathogens hijack the host basal transcription factors TFIIAα and TFIIAγ, but not TFIIAß, to enhance host susceptibility during pathogen infection. The uncovered mechanism widens new insights on host-microbe interaction and provide an applicable strategy to breed high-resistance crop varieties.
[Mh] Termos MeSH primário: Interações Hospedeiro-Patógeno
Oryza/microbiologia
Doenças das Plantas/microbiologia
Proteínas de Plantas/metabolismo
Efetores Semelhantes a Ativadores de Transcrição/metabolismo
Fator de Transcrição TFIIA/metabolismo
Xanthomonas/fisiologia
[Mh] Termos MeSH secundário: Resistência à Doença
Regulação da Expressão Gênica de Plantas
Genes de Plantas
Oryza/genética
Oryza/metabolismo
Doenças das Plantas/genética
Ligação Proteica
Subunidades Proteicas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Plant Proteins); 0 (Protein Subunits); 0 (Transcription Activator-Like Effectors); 0 (Transcription Factor TFIIA)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180115
[St] Status:MEDLINE


  2 / 21761 MEDLINE  
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[PMID]:29311697
[Au] Autor:Qureshi BM; Schmidt A; Behrmann E; Bürger J; Mielke T; Spahn CMT; Heck M; Scheerer P
[Ad] Endereço:Charité - Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Charitéplatz 1, D-10117, Berlin, Germany.
[Ti] Título:Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6.
[So] Source:Nat Commun;9(1):90, 2018 01 08.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Isoprenylated proteins are associated with membranes and their inter-compartmental distribution is regulated by solubilization factors, which incorporate lipid moieties in hydrophobic cavities and thereby facilitate free diffusion during trafficking. Here we report the crystal structure of a solubilization factor, the prenyl-binding protein (PrBP/δ), at 1.81 Å resolution in its ligand-free apo-form. Apo-PrBP/δ harbors a preshaped, deep hydrophobic cavity, capacitating apo-PrBP/δ to readily bind its prenylated cargo. To investigate the molecular mechanism of cargo solubilization we analyzed the PrBP/δ-induced membrane dissociation of rod photoreceptor phosphodiesterase (PDE6). The results suggest that PrBP/δ exclusively interacts with the soluble fraction of PDE6. Depletion of soluble species in turn leads to dissociation of membrane-bound PDE6, as both are in equilibrium. This "solubilization by depletion" mechanism of PrBP/δ differs from the extraction of prenylated proteins by the similar folded solubilization factor RhoGDI, which interacts with membrane bound cargo via an N-terminal structural element lacking in PrBP/δ.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Nucleotídeo Cíclico Fosfodiesterase do Tipo 6/metabolismo
Neopreno/metabolismo
Células Fotorreceptoras Retinianas Bastonetes/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte/química
Bovinos
Cristalografia por Raios X
Nucleotídeo Cíclico Fosfodiesterase do Tipo 6/química
Modelos Moleculares
Complexos Multiproteicos/química
Complexos Multiproteicos/metabolismo
Neopreno/química
Ligação Proteica
Domínios Proteicos
Prenilação de Proteína
Subunidades Proteicas/química
Subunidades Proteicas/metabolismo
Inibidores da Dissociação do Nucleotídeo Guanina rho-Específico/química
Inibidores da Dissociação do Nucleotídeo Guanina rho-Específico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Multiprotein Complexes); 0 (Protein Subunits); 0 (prenyl); 0 (rho-Specific Guanine Nucleotide Dissociation Inhibitors); 9010-98-4 (Neoprene); EC 3.1.4.35 (Cyclic Nucleotide Phosphodiesterases, Type 6)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180110
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02569-y


  3 / 21761 MEDLINE  
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[PMID]:29311594
[Au] Autor:Nakanishi A; Kishikawa JI; Tamakoshi M; Mitsuoka K; Yokoyama K
[Ad] Endereço:Department of Molecular Biosciences, Kyoto Sangyo University, Motoyama Kamigamo, Kita-ku, Kyoto, 603-8555, Japan.
[Ti] Título:Cryo EM structure of intact rotary H -ATPase/synthase from Thermus thermophilus.
[So] Source:Nat Commun;9(1):89, 2018 01 08.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Proton translocating rotary ATPases couple ATP hydrolysis/synthesis, which occurs in the soluble domain, with proton flow through the membrane domain via a rotation of the common central rotor complex against the surrounding peripheral stator apparatus. Here, we present a large data set of single particle cryo-electron micrograph images of the V/A type H -rotary ATPase from the bacterium Thermus thermophilus, enabling the identification of three rotational states based on the orientation of the rotor subunit. Using masked refinement and classification with signal subtractions, we obtain homogeneous reconstructions for the whole complexes and soluble V domains. These reconstructions are of higher resolution than any EM map of intact rotary ATPase reported previously, providing a detailed molecular basis for how the rotary ATPase maintains structural integrity of the peripheral stator apparatus, and confirming the existence of a clear proton translocation path from both sides of the membrane.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Proteínas de Bactérias/metabolismo
Thermus thermophilus/enzimologia
ATPases Vacuolares Próton-Translocadoras/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/ultraestrutura
Transporte Biológico
Microscopia Crioeletrônica
Hidrólise
Modelos Moleculares
Conformação Proteica
Subunidades Proteicas/química
Subunidades Proteicas/metabolismo
Prótons
Rotação
ATPases Vacuolares Próton-Translocadoras/química
ATPases Vacuolares Próton-Translocadoras/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Protein Subunits); 0 (Protons); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Vacuolar Proton-Translocating ATPases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180110
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02553-6


  4 / 21761 MEDLINE  
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[PMID]:29352320
[Au] Autor:Zhou X; Desai R; Zhang Y; Stec WJ; Miller KW; Jounaidi Y
[Ad] Endereço:Department of Anesthesia, Critical Care and Pain Medicine, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts, United States of America.
[Ti] Título:High-level production and purification in a functional state of an extrasynaptic gamma-aminobutyric acid type A receptor containing α4ß3δ subunits.
[So] Source:PLoS One;13(1):e0191583, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The inhibitory γ-aminobutyric acid type A receptors are implicated in numerous physiological processes, including cognition and inhibition of neurotransmission, rendering them important molecular targets for many classes of drugs. Functionally, the entire GABAAR family of receptors can be subdivided into phasic, fast acting synaptic receptors, composed of α-, ß- and γ-subunits, and tonic extrasynaptic receptors, many of which contain the δ-subunit in addition to α- and ß-subunits. Whereas the subunit arrangement of the former group is agreed upon, that of the αßδ GABAARs remains unresolved by electrophysiological and pharmacological research. To resolve such issues will require biophysical techniques that demand quantities of receptor that have been previously unavailable. Therefore, we have engineered a stable cell line with tetracycline inducible expression of human α4-, ß3- and N-terminally Flag-tagged δ-subunits. This cell line achieved a specific activity between 15 and 20 pmol [3H]muscimol sites/mg of membrane protein, making it possible to obtain 1 nmole of purified α4ß3δ GABAAR from sixty 15-cm culture dishes. When induced, these cells exhibited agonist-induced currents with characteristics comparable to those previously reported for this receptor and a pharmacology that included strong modulation by etomidate and the δ-subunit-specific ligand, DS2. Immunoaffinity purification and reconstitution in CHAPS/asolectin micelles resulted in the retention of equilibrium allosteric interactions between the separate agonist, anesthetic and DS2 sites. Moreover, all three subunits retained glycosylation. The establishment of this well-characterized cell line will allow molecular level studies of tonic receptors to be undertaken.
[Mh] Termos MeSH primário: Receptores de GABA-A/biossíntese
[Mh] Termos MeSH secundário: Fenômenos Eletrofisiológicos
Células HEK293
Seres Humanos
Cinética
Engenharia de Proteínas
Subunidades Proteicas
Ensaio Radioligante
Receptores de GABA-A/genética
Receptores de GABA-A/isolamento & purificação
Proteínas Recombinantes de Fusão/biossíntese
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/isolamento & purificação
Transfecção
Ácido gama-Aminobutírico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protein Subunits); 0 (Receptors, GABA-A); 0 (Recombinant Fusion Proteins); 56-12-2 (gamma-Aminobutyric Acid)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180121
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191583


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[PMID]:29339073
[Au] Autor:Roginski RS; Lau CW; Santoiemma PP; Weaver SJ; Du P; Soteropoulos P; Yang J
[Ad] Endereço:Department of Anesthesiology, CMC VA Medical Center, Philadelphia, PA 19104, United States; Department of Anesthesiology and Critical Care, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, United States. Electronic address: raymond.roginski@va.gov.
[Ti] Título:The human GCOM1 complex gene interacts with the NMDA receptor and internexin-alpha.
[So] Source:Gene;648:42-53, 2018 Mar 30.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The known functions of the human GCOM1 complex hub gene include transcription elongation and the intercalated disk of cardiac myocytes. However, in all likelihood, the gene's most interesting, and thus far least understood, roles will be found in the central nervous system. To investigate the functions of the GCOM1 gene in the CNS, we have cloned human and rat brain cDNAs encoding novel, 105 kDa GCOM1 combined (Gcom) proteins, designated Gcom15, and identified a new group of GCOM1 interacting genes, termed Gints, from yeast two-hybrid (Y2H) screens. We showed that Gcom15 interacts with the NR1 subunit of the NMDA receptor by co-expression in heterologous cells, in which we observed bi-directional co-immunoprecipitation of human Gcom15 and murine NR1. Our Y2H screens revealed 27 novel GCOM1 interacting genes, many of which are synaptic proteins and/or play roles in neurologic diseases. Finally, we showed, using rat brain protein preparations, that the Gint internexin-alpha (INA), a known interactor of the NMDAR, co-IPs with GCOM1 proteins, suggesting a GCOM1-GRIN1-INA interaction and a novel pathway that may be relevant to neuroprotection.
[Mh] Termos MeSH primário: Proteínas de Filamentos Intermediários/metabolismo
RNA Polimerase II/metabolismo
Receptores de N-Metil-D-Aspartato/metabolismo
[Mh] Termos MeSH secundário: Adulto
Animais
Encéfalo/metabolismo
Células HEK293
Seres Humanos
Imunoprecipitação
Proteínas de Filamentos Intermediários/genética
Masculino
Camundongos
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Ligação Proteica
Mapas de Interação de Proteínas
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
RNA Polimerase II/genética
Ratos Wistar
Receptores de N-Metil-D-Aspartato/genética
Técnicas do Sistema de Duplo-Híbrido
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GRIN1 protein, human); 0 (Intermediate Filament Proteins); 0 (NR1 NMDA receptor); 0 (Nerve Tissue Proteins); 0 (POLR2M protein, human); 0 (Protein Subunits); 0 (Receptors, N-Methyl-D-Aspartate); 0 (alpha-internexin); EC 2.7.7.- (RNA Polymerase II)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE


  6 / 21761 MEDLINE  
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[PMID]:27773677
[Au] Autor:Jeronimo C; Langelier MF; Bataille AR; Pascal JM; Pugh BF; Robert F
[Ad] Endereço:Institut de recherches cliniques de Montréal, 110 Avenue des Pins Ouest, Montréal, QC H2W 1R7, Canada.
[Ti] Título:Tail and Kinase Modules Differently Regulate Core Mediator Recruitment and Function In Vivo.
[So] Source:Mol Cell;64(3):455-466, 2016 Nov 03.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mediator is a highly conserved transcriptional coactivator organized into four modules, namely Tail, Middle, Head, and Kinase (CKM). Previous work suggests regulatory roles for Tail and CKM, but an integrated model for these activities is lacking. Here, we analyzed the genome-wide distribution of Mediator subunits in wild-type and mutant yeast cells in which RNA polymerase II promoter escape is blocked, allowing detection of transient Mediator forms. We found that although all modules are recruited to upstream activated regions (UAS), assembly of Mediator within the pre-initiation complex is accompanied by the release of CKM. Interestingly, our data show that CKM regulates Mediator-UAS interaction rather than Mediator-promoter association. In addition, although Tail is required for Mediator recruitment to UAS, Tailless Mediator nevertheless interacts with core promoters. Collectively, our data suggest that the essential function of Mediator is mediated by Head and Middle at core promoters, while Tail and CKM play regulatory roles.
[Mh] Termos MeSH primário: Regulação Fúngica da Expressão Gênica
Complexo Mediador/genética
RNA Polimerase II/genética
Proteínas de Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/genética
Fator de Transcrição TFIIB/genética
[Mh] Termos MeSH secundário: Sítios de Ligação
Complexo Mediador/metabolismo
Modelos Moleculares
Regiões Promotoras Genéticas
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
RNA Polimerase II/metabolismo
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Fator de Transcrição TFIIB/metabolismo
Iniciação da Transcrição Genética
Ativação Transcricional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mediator Complex); 0 (Protein Subunits); 0 (SUA7 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factor TFIIB); EC 2.7.7.- (RNA Polymerase II)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161105
[St] Status:MEDLINE


  7 / 21761 MEDLINE  
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[PMID]:28468258
[Au] Autor:Federico A; Rienzo M; Abbondanza C; Costa V; Ciccodicola A; Casamassimi A
[Ad] Endereço:Institute of Genetics and Biophysics "Adriano Buzzati Traverso", CNR, 80131 Naples, Italy. antonio.federico@igb.cnr.it.
[Ti] Título:Pan-Cancer Mutational and Transcriptional Analysis of the Integrator Complex.
[So] Source:Int J Mol Sci;18(5), 2017 Apr 29.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The integrator complex has been recently identified as a key regulator of RNA Polymerase II-mediated transcription, with many functions including the processing of small nuclear RNAs, the pause-release and elongation of polymerase during the transcription of protein coding genes, and the biogenesis of enhancer derived transcripts. Moreover, some of its components also play a role in genome maintenance. Thus, it is reasonable to hypothesize that their functional impairment or altered expression can contribute to malignancies. Indeed, several studies have described the mutations or transcriptional alteration of some Integrator genes in different cancers. Here, to draw a comprehensive pan-cancer picture of the genomic and transcriptomic alterations for the members of the complex, we reanalyzed public data from The Cancer Genome Atlas. Somatic mutations affecting Integrator subunit genes and their transcriptional profiles have been investigated in about 11,000 patients and 31 tumor types. A general heterogeneity in the mutation frequencies was observed, mostly depending on tumor type. Despite the fact that we could not establish them as cancer drivers, and genes were highly mutated in specific cancers. A transcriptome analysis of paired (normal and tumor) samples revealed that the transcription of , , and is significantly altered in several cancers. Experimental validation performed on primary tumors confirmed these findings.
[Mh] Termos MeSH primário: Regulação Neoplásica da Expressão Gênica
Neoplasias/genética
Subunidades Proteicas/genética
[Mh] Termos MeSH secundário: Perfilação da Expressão Gênica
Genoma Humano
Genômica
Seres Humanos
Mutação
Transcrição Genética
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (INTS8 protein, human); 0 (Protein Subunits)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


  8 / 21761 MEDLINE  
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[PMID]:29217583
[Au] Autor:Yin Y; Wu M; Zubcevic L; Borschel WF; Lander GC; Lee SY
[Ad] Endereço:Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA.
[Ti] Título:Structure of the cold- and menthol-sensing ion channel TRPM8.
[So] Source:Science;359(6372):237-241, 2018 01 12.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Transient receptor potential melastatin (TRPM) cation channels are polymodal sensors that are involved in a variety of physiological processes. Within the TRPM family, member 8 (TRPM8) is the primary cold and menthol sensor in humans. We determined the cryo-electron microscopy structure of the full-length TRPM8 from the collared flycatcher at an overall resolution of ~4.1 ångstroms. Our TRPM8 structure reveals a three-layered architecture. The amino-terminal domain with a fold distinct among known TRP structures, together with the carboxyl-terminal region, forms a large two-layered cytosolic ring that extensively interacts with the transmembrane channel layer. The structure suggests that the menthol-binding site is located within the voltage-sensor-like domain and thus provides a structural glimpse of the design principle of the molecular transducer for cold and menthol sensation.
[Mh] Termos MeSH primário: Proteínas Aviárias/química
Mentol/metabolismo
Passeriformes/metabolismo
Canais de Cátion TRPM/química
[Mh] Termos MeSH secundário: Animais
Proteínas Aviárias/metabolismo
Proteínas Aviárias/ultraestrutura
Sítios de Ligação
Temperatura Baixa
Microscopia Crioeletrônica
Processamento de Imagem Assistida por Computador
Modelos Moleculares
Domínios Proteicos
Dobramento de Proteína
Estrutura Secundária de Proteína
Subunidades Proteicas
Canais de Cátion TRPM/metabolismo
Canais de Cátion TRPM/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Avian Proteins); 0 (Protein Subunits); 0 (TRPM Cation Channels); 1490-04-6 (Menthol)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE
[do] DOI:10.1126/science.aan4325


  9 / 21761 MEDLINE  
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[PMID]:28454681
[Au] Autor:Trachana V; Petrakis S; Fotiadis Z; Siska EK; Balis V; Gonos ES; Kaloyianni M; Koliakos G
[Ad] Endereço:Laboratory of Biology, Faculty of Medicine, School of Health Sciences, University of Thessaly, 41500 Larisa, Greece. Electronic address: vtrachana@med.uth.gr.
[Ti] Título:Human mesenchymal stem cells with enhanced telomerase activity acquire resistance against oxidative stress-induced genomic damage.
[So] Source:Cytotherapy;19(7):808-820, 2017 07.
[Is] ISSN:1477-2566
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Human mesenchymal stem cells (MSC) are important tools for several cell-based therapies. However, their use in such therapies requires in vitro expansion during which MSCs quickly reach replicative senescence. Replicative senescence has been linked to macromolecular damage, and especially oxidative stress-induced DNA damage. Recent studies on the other hand, have implicated telomerase in the cellular response to oxidative damage, suggesting that telomerase has a telomere-length independent function that promotes survival. METHODS: Here, we studied the DNA damage accumulation and repair during in vitro expansion as well as after acute external oxidative exposure of control MSCs and MSCs that overexpress the catalytic subunit of telomerase (hTERT MSCs). RESULTS: We showed that hTERT MSCs at high passages have a significant lower percentage of DNA lesions as compared to control cells of the same passages. Additionally, less damage was accumulated due to external oxidative insult in the nuclei of hTERT overexpressing cells as compared to the control cells. Moreover, we demonstrated that oxidative stress leads to diverse nucleus malformations, such as multillobular nuclei or donut-shaped nuclei, in the control cells whereas hTERT MSCs showed significant resistance to the formation of such defects. Finally, hTERT MSCs were found to possess higher activities of the basic antioxidant enzymes, superoxide dismutase and catalase, than control MSCs. DISCUSSION: On the basis of these results, we propose that hTERT enhancement confers resistance to genomic damage due to the amelioration of the cell's basic antioxidant machinery.
[Mh] Termos MeSH primário: Antioxidantes/metabolismo
Dano ao DNA
Células Mesenquimais Estromais/fisiologia
Estresse Oxidativo
Telomerase/metabolismo
[Mh] Termos MeSH secundário: Catalase/metabolismo
Células Cultivadas
Senescência Celular/fisiologia
Seres Humanos
Peróxido de Hidrogênio/farmacologia
Células Mesenquimais Estromais/efeitos dos fármacos
Estresse Oxidativo/efeitos dos fármacos
Subunidades Proteicas
Superóxido Dismutase/metabolismo
Telomerase/genética
Telômero
Homeostase do Telômero
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Protein Subunits); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.6 (Catalase); EC 1.15.1.1 (Superoxide Dismutase); EC 2.7.7.49 (Telomerase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE


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[PMID]:29364597
[Au] Autor:Solov'ev AA; Ashikhmin AA; Moskalenko AA
[Ti] Título:Formation of a Subunit Form of the Core Light-Harvesting Complex from Sulfur Purple Bacteria Ectothiorhodospira haloalkaliphila with Different Carotenoid Composition.
[So] Source:Mikrobiologiia;85(5):497-505, 2016 Sep.
[Is] ISSN:0026-3656
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:B820 subunits from a purple sulfur bacterium Ectothiorhodospira. haloalkaliphila strain ATCC 51935T were obtained by treatment of Carotenoid free LH I-RC complexes of this bacterium with P--octylglu- copyranoside (ß-OG). The same complexes with 100% carotenoid content were unable to dissociate to B820 subunits, but disintegrated to monomeric bacteriochlorophyll (BChl) regardless of their carotenoid compo- sition. The degree of dissociation of the LH 1-RC complexes with an intermediate content of carotenoids (the' B820 formation) was directly dependent on the quantity of carotenoids in the samples. The resulting B820 subunits did not contain carotenoids. B820 subunits easily aggregated to form a complex with an absorption . peak at 880 nm at decreased ß-OG concentration. Analysis of the spectra of the LH I-RC complexes isolated from the cells with different'levels of carotenogenesis inhibition led to the conclusion of the heterogeneity of the samples with a predominance in them of (a) the fraction with 100% of carotenoids and (b) the fraction of carotenoid free complexes.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Carotenoides/isolamento & purificação
Chromatiaceae/química
Ectothiorhodospiraceae/química
Complexos de Proteínas Captadores de Luz/química
Subunidades Proteicas/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/isolamento & purificação
Bacterioclorofilas/química
Bacterioclorofilas/isolamento & purificação
Carotenoides/química
Carotenoides/classificação
Chromatiaceae/metabolismo
Detergentes/química
Ectothiorhodospiraceae/metabolismo
Glucosídeos/química
Complexos de Proteínas Captadores de Luz/isolamento & purificação
Extração Líquido-Líquido/métodos
Agregados Proteicos
Subunidades Proteicas/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Bacteriochlorophylls); 0 (Detergents); 0 (Glucosides); 0 (Light-Harvesting Protein Complexes); 0 (Protein Aggregates); 0 (Protein Subunits); 29836-26-8 (octyl-beta-D-glucoside); 36-88-4 (Carotenoids)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180125
[St] Status:MEDLINE



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