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[PMID]:28470608
[Au] Autor:Raran-Kurussi S; Cherry S; Zhang D; Waugh DS
[Ad] Endereço:Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, B, Frederick, MD, 21702-1201, USA.
[Ti] Título:Removal of Affinity Tags with TEV Protease.
[So] Source:Methods Mol Biol;1586:221-230, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Although affinity tags are highly effective tools for the expression and purification of recombinant proteins, they generally need to be removed prior to structural and functional studies. This chapter describes a simple method for overproducing a soluble form of a stable variant of tobacco etch virus (TEV) protease in Escherichia coli and a protocol for purifying it to homogeneity so that it can be used as a reagent for removing affinity tags from recombinant proteins by site-specific endoproteolysis. Further, we cleave a model substrate protein (MBP-NusG) in vitro using the purified TEV protease to illustrate a protease cleavage protocol that can be employed for simple pilot experiments and large-scale protein preparations.
[Mh] Termos MeSH primário: Cromatografia de Afinidade/métodos
Endopeptidases/genética
Endopeptidases/isolamento & purificação
Escherichia coli/genética
Potyvirus/enzimologia
[Mh] Termos MeSH secundário: Clonagem Molecular/métodos
Endopeptidases/metabolismo
Escherichia coli/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Proteínas Ligantes de Maltose/genética
Proteínas Ligantes de Maltose/metabolismo
Fatores de Alongamento de Peptídeos/genética
Fatores de Alongamento de Peptídeos/metabolismo
Proteólise
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/isolamento & purificação
Proteínas Recombinantes de Fusão/metabolismo
Solubilidade
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Maltose-Binding Proteins); 0 (NusG protein, E coli); 0 (Peptide Elongation Factors); 0 (Recombinant Fusion Proteins); 0 (Transcription Factors); EC 3.4.- (Endopeptidases); EC 3.4.- (TEV protease)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6887-9_14


  2 / 3189 MEDLINE  
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[PMID]:29300771
[Au] Autor:Mateyak MK; Pupek JK; Garino AE; Knapp MC; Colmer SF; Kinzy TG; Dunaway S
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers, the State University of New Jersey, Piscataway, NJ, United States of America.
[Ti] Título:Demonstration of translation elongation factor 3 activity from a non-fungal species, Phytophthora infestans.
[So] Source:PLoS One;13(1):e0190524, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In most eukaryotic organisms, translation elongation requires two highly conserved elongation factors eEF1A and eEF2. Fungal systems are unique in requiring a third factor, the eukaryotic Elongation Factor 3 (eEF3). For decades, eEF3, a ribosome-dependent ATPase, was considered "fungal-specific", however, recent bioinformatics analysis indicates it may be more widely distributed among other unicellular eukaryotes. In order to determine whether divergent eEF3-like proteins from other eukaryotic organisms can provide the essential functions of eEF3 in budding yeast, the eEF3-like proteins from Schizosaccharomyes pombe and an oomycete, Phytophthora infestans, were cloned and expressed in Saccharomyces cerevisiae. Plasmid shuffling experiments showed that both S. pombe and P. infestans eEF3 can support the growth of S. cerevisiae in the absence of endogenous budding yeast eEF3. Consistent with its ability to provide the essential functions of eEF3, P. infestans eEF3 possessed ribosome-dependent ATPase activity. Yeast cells expressing P. infestans eEF3 displayed reduced protein synthesis due to defects in translation elongation/termination. Identification of eEF3 in divergent species will advance understanding of its function and the ribosome specific determinants that lead to its requirement as well as contribute to the identification of functional domains of eEF3 for potential drug discovery.
[Mh] Termos MeSH primário: Fatores de Alongamento de Peptídeos/metabolismo
Phytophthora infestans/metabolismo
[Mh] Termos MeSH secundário: Elongação Traducional da Cadeia Peptídica
Fatores de Alongamento de Peptídeos/classificação
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Peptide Elongation Factors)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180105
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190524


  3 / 3189 MEDLINE  
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[PMID]:29227074
[Au] Autor:Minchenko OH; Tsymbal DO; Minchenko DO; Riabovol OO; Ratushna OO; Karbovskyi LL
[Ti] Título:Hypoxic regulation of the expression of cell proliferation related genes in U87 glioma cells upon inhibition of ire1 signaling enzyme
[So] Source:Ukr Biochem J;88(1):11-21, 2016 Ja-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:We have studied the effect of inhibition of IRE1 (inositol requiring enzyme 1), which is a central mediator of endoplasmic reticulum stress and a controller of cell proliferation and tumor growth, on hypoxic regulation of the expression of different proliferation related genes in U87 glioma cells. It was shown that hypoxia leads to up-regulation of the expression of IL13RA2, CD24, ING1, ING2, ENDOG, and POLG genes and to down-regulation ­ of KRT18, TRAPPC3, TSFM, and MTIF2 genes at the mRNA level in control glioma cells. Changes for ING1 and CD24 genes were more significant. At the same time, inhibition of IRE1 modifies the effect of hypoxia on the expression of all studied genes. In particular, it increases sensitivity to hypoxia of the expression of IL13RA2, TRAPPC3, ENDOG, and PLOG genes and suppresses the effect of hypoxia on the expression of ING1 gene. Additionally, it eliminates hypoxic regulation of KRT18, CD24, ING2, TSFM, and MTIF2 genes expressions and introduces sensitivity to hypoxia of the expression of BET1 gene in glioma cells. The present study demonstrates that hypoxia, which often contributes to tumor growth, affects the expression of almost all studied genes. Additionally, inhibition of IRE1 can both enhance and suppress the hypoxic regulation of these gene expressions in a gene specific manner and thus possibly contributes to slower glioma growth, but several aspects of this regulation must be further clarified.
[Mh] Termos MeSH primário: Estresse do Retículo Endoplasmático/genética
Endorribonucleases/genética
Regulação Neoplásica da Expressão Gênica
Neuroglia/metabolismo
Proteínas Serina-Treonina Quinases/genética
RNA Mensageiro/genética
Transdução de Sinais/genética
[Mh] Termos MeSH secundário: Antígeno CD24/genética
Antígeno CD24/metabolismo
Hipóxia Celular
Linhagem Celular Tumoral
Proliferação Celular
DNA Polimerase gama/genética
DNA Polimerase gama/metabolismo
Endodesoxirribonucleases/genética
Endodesoxirribonucleases/metabolismo
Endorribonucleases/antagonistas & inibidores
Endorribonucleases/metabolismo
Fatores de Iniciação em Eucariotos/genética
Fatores de Iniciação em Eucariotos/metabolismo
Proteínas de Homeodomínio/genética
Proteínas de Homeodomínio/metabolismo
Seres Humanos
Proteína 1 Inibidora do Crescimento/genética
Proteína 1 Inibidora do Crescimento/metabolismo
Subunidade alfa2 de Receptor de Interleucina-13/genética
Subunidade alfa2 de Receptor de Interleucina-13/metabolismo
Queratina-18/genética
Queratina-18/metabolismo
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
Neuroglia/patologia
Fatores de Alongamento de Peptídeos/genética
Fatores de Alongamento de Peptídeos/metabolismo
Proteínas Serina-Treonina Quinases/antagonistas & inibidores
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas Qc-SNARE/genética
Proteínas Qc-SNARE/metabolismo
RNA Mensageiro/metabolismo
Receptores Citoplasmáticos e Nucleares/genética
Receptores Citoplasmáticos e Nucleares/metabolismo
Proteínas Supressoras de Tumor/genética
Proteínas Supressoras de Tumor/metabolismo
Proteínas de Transporte Vesicular/genética
Proteínas de Transporte Vesicular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BET1L protein, human); 0 (CD24 Antigen); 0 (Eukaryotic Initiation Factors); 0 (Homeodomain Proteins); 0 (ING1 protein, human); 0 (ING2 protein, human); 0 (Inhibitor of Growth Protein 1); 0 (Interleukin-13 Receptor alpha2 Subunit); 0 (KRT18 protein, human); 0 (Keratin-18); 0 (MTIF2 protein, human); 0 (Mitochondrial Proteins); 0 (Peptide Elongation Factors); 0 (Qc-SNARE Proteins); 0 (RNA, Messenger); 0 (Receptors, Cytoplasmic and Nuclear); 0 (TRAPPC3 protein, human); 0 (TSFM protein, human); 0 (Tumor Suppressor Proteins); 0 (Vesicular Transport Proteins); EC 2.7.11.1 (ERN1 protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.7.7 (DNA Polymerase gamma); EC 2.7.7.7 (POLG protein, human); EC 3.1.- (Endodeoxyribonucleases); EC 3.1.- (Endoribonucleases); EC 3.1.21.- (endonuclease G)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.01.011


  4 / 3189 MEDLINE  
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[PMID]:29028845
[Au] Autor:Shamsuzzaman M; Bommakanti A; Zapinsky A; Rahman N; Pascual C; Lindahl L
[Ad] Endereço:Department of Biological Sciences, University of Maryland Baltimore County (UMBC), Baltimore, Maryland, United States of America.
[Ti] Título:Analysis of cell cycle parameters during the transition from unhindered growth to ribosomal and translational stress conditions.
[So] Source:PLoS One;12(10):e0186494, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Abrogation of ribosome synthesis (ribosomal stress) leads to cell cycle arrest. However, the immediate cell response to cessation of ribosome formation and the transition from normal cell proliferation to cell cycle arrest have not been characterized. Furthermore, there are conflicting conclusions about whether cells are arrested in G2/M or G1, and whether the cause is dismantling ribosomal assembly per se, or the ensuing decreased number of translating ribosomes. To address these questions, we have compared the time kinetics of key cell cycle parameters after inhibiting ribosome formation or function in Saccharomyces cerevisiae. Within one-to-two hours of repressing genes for individual ribosomal proteins or Translation Elongation factor 3, configurations of spindles, spindle pole bodies began changing. Actin began depolarizing within 4 hours. Thus the loss of ribosome formation and function is sensed immediately. After several hours no spindles or mitotic actin rings were visible, but membrane ingression was completed in most cells and Ace2 was localized to daughter cell nuclei demonstrating that the G1 stage was reached. Thus cell division was completed without the help of a contractile actin ring. Moreover, cell wall material held mother and daughter cells together resulting in delayed cell separation, suggesting that expression or function of daughter gluconases and chitinases is inhibited. Moreover, cell development changes in very similar ways in response to inhibition of ribosome formation and function, compatible with the notion that decreased translation capacity contributes to arresting the cell cycle after abrogation of ribosome biogenesis. Potential implications for the mechanisms of diseases caused by mutations in ribosomal genes (ribosomopathies) are discussed.
[Mh] Termos MeSH primário: Ciclo Celular
Biossíntese de Proteínas
Ribossomos/genética
Saccharomyces cerevisiae/citologia
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Actinas/metabolismo
Parede Celular/metabolismo
Proteínas de Ligação a DNA/metabolismo
Fatores de Alongamento de Peptídeos/metabolismo
Ribossomos/metabolismo
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Fuso Acromático/metabolismo
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ACE2 protein, S cerevisiae); 0 (Actins); 0 (DNA-Binding Proteins); 0 (Peptide Elongation Factors); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factors); 0 (YEF3 protein, S cerevisiae)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171014
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186494


  5 / 3189 MEDLINE  
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[PMID]:28886186
[Au] Autor:Estrada-Avilés R; Rodríguez G; Zarain-Herzberg A
[Ad] Endereço:Department of Biochemistry, School of Medicine, National Autonomous University of Mexico, Mexico City, Mexico.
[Ti] Título:The cardiac calsequestrin gene transcription is modulated at the promoter by NFAT and MEF-2 transcription factors.
[So] Source:PLoS One;12(9):e0184724, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Calsequestrin-2 (CASQ2) is the main Ca2+-binding protein inside the sarcoplasmic reticulum of cardiomyocytes. Previously, we demonstrated that MEF-2 and SRF binding sites within the human CASQ2 gene (hCASQ2) promoter region are functional in neonatal cardiomyocytes. In this work, we investigated if the calcineurin/NFAT pathway regulates hCASQ2 expression in neonatal cardiomyocytes. The inhibition of NFAT dephosphorylation with CsA or INCA-6, reduced both the luciferase activity of hCASQ2 promoter constructs (-3102/+176 bp and -288/+176 bp) and the CASQ2 mRNA levels in neonatal rat cardiomyocytes. Additionally, NFATc1 and NFATc3 over-expressing neonatal cardiomyocytes showed a 2-3-fold increase in luciferase activity of both hCASQ2 promoter constructs, which was prevented by CsA treatment. Site-directed mutagenesis of the -133 bp MEF-2 binding site prevented trans-activation of hCASQ2 promoter constructs induced by NFAT overexpression. Chromatin Immunoprecipitation (ChIP) assays revealed NFAT and MEF-2 enrichment within the -288 bp to +76 bp of the hCASQ2 gene promoter. Besides, a direct interaction between NFAT and MEF-2 proteins was demonstrated by protein co-immunoprecipitation experiments. Taken together, these data demonstrate that NFAT interacts with MEF-2 bound to the -133 bp binding site at the hCASQ2 gene promoter. In conclusion, in this work, we demonstrate that the Ca2+-calcineurin/NFAT pathway modulates the transcription of the hCASQ2 gene in neonatal cardiomyocytes.
[Mh] Termos MeSH primário: Calsequestrina/genética
Calsequestrina/metabolismo
Regiões Promotoras Genéticas/genética
[Mh] Termos MeSH secundário: Animais
Western Blotting
Calcineurina/genética
Calcineurina/metabolismo
Células Cultivadas
Imunoprecipitação da Cromatina
Mutagênese Sítio-Dirigida
Miócitos Cardíacos/metabolismo
Fatores de Transcrição NFATC/genética
Fatores de Transcrição NFATC/metabolismo
Fatores de Alongamento de Peptídeos/genética
Fatores de Alongamento de Peptídeos/metabolismo
Ligação Proteica/genética
Ligação Proteica/fisiologia
Ratos
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Transdução de Sinais/genética
Transdução de Sinais/fisiologia
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calsequestrin); 0 (NFATC Transcription Factors); 0 (NFATC1 protein, rat); 0 (Peptide Elongation Factors); 0 (Transcription Factors); 0 (calsequestrin 2, rat); EC 3.1.3.16 (Calcineurin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184724


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[PMID]:28877031
[Au] Autor:Zhang G; Feenstra B; Bacelis J; Liu X; Muglia LM; Juodakis J; Miller DE; Litterman N; Jiang PP; Russell L; Hinds DA; Hu Y; Weirauch MT; Chen X; Chavan AR; Wagner GP; Pavlicev M; Nnamani MC; Maziarz J; Karjalainen MK; Rämet M; Sengpiel V; Geller F; Boyd HA; Palotie A; Momany A; Bedell B; Ryckman KK; Huusko JM; Forney CR; Kottyan LC; Hallman M; Teramo K; Nohr EA; Davey Smith G; Melbye M; Jacobsson B; Muglia LJ
[Ad] Endereço:From the Division of Human Genetics (G.Z., L.J.M.), Center for Autoimmune Genomics and Etiology (M.T.W., D.E.M., X.C., C.R.F., L.C.K.) and the Divisions of Biomedical Informatics and Developmental Biology (M.T.W.), Cincinnati Children's Hospital Medical Center, and the Center for Prevention of Prete
[Ti] Título:Genetic Associations with Gestational Duration and Spontaneous Preterm Birth.
[So] Source:N Engl J Med;377(12):1156-1167, 2017 09 21.
[Is] ISSN:1533-4406
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Despite evidence that genetic factors contribute to the duration of gestation and the risk of preterm birth, robust associations with genetic variants have not been identified. We used large data sets that included the gestational duration to determine possible genetic associations. METHODS: We performed a genomewide association study in a discovery set of samples obtained from 43,568 women of European ancestry using gestational duration as a continuous trait and term or preterm (<37 weeks) birth as a dichotomous outcome. We used samples from three Nordic data sets (involving a total of 8643 women) to test for replication of genomic loci that had significant genomewide association (P<5.0×10 ) or an association with suggestive significance (P<1.0×10 ) in the discovery set. RESULTS: In the discovery and replication data sets, four loci (EBF1, EEFSEC, AGTR2, and WNT4) were significantly associated with gestational duration. Functional analysis showed that an implicated variant in WNT4 alters the binding of the estrogen receptor. The association between variants in ADCY5 and RAP2C and gestational duration had suggestive significance in the discovery set and significant evidence of association in the replication sets; these variants also showed genomewide significance in a joint analysis. Common variants in EBF1, EEFSEC, and AGTR2 showed association with preterm birth with genomewide significance. An analysis of mother-infant dyads suggested that these variants act at the level of the maternal genome. CONCLUSIONS: In this genomewide association study, we found that variants at the EBF1, EEFSEC, AGTR2, WNT4, ADCY5, and RAP2C loci were associated with gestational duration and variants at the EBF1, EEFSEC, and AGTR2 loci with preterm birth. Previously established roles of these genes in uterine development, maternal nutrition, and vascular control support their mechanistic involvement. (Funded by the March of Dimes and others.).
[Mh] Termos MeSH primário: Predisposição Genética para Doença
Variação Genética
Idade Gestacional
Fatores de Alongamento de Peptídeos/genética
Nascimento Prematuro/genética
Receptor Tipo 2 de Angiotensina/genética
Transativadores/genética
[Mh] Termos MeSH secundário: Adenilil Ciclases/genética
Conjuntos de Dados como Assunto
Feminino
Estudo de Associação Genômica Ampla
Seres Humanos
Fenótipo
Polimorfismo de Nucleotídeo Único
Gravidez
Análise de Regressão
Proteína Wnt4/genética
Proteínas ras/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 (EBF1 protein, human); 0 (EEFSEC protein, human); 0 (Peptide Elongation Factors); 0 (Receptor, Angiotensin, Type 2); 0 (Trans-Activators); 0 (Wnt4 Protein); EC 3.6.1.- (Rap2C protein, human); EC 3.6.5.2 (ras Proteins); EC 4.6.1.1 (Adenylyl Cyclases); EC 4.6.1.1 (adenylyl cyclase type V)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171122
[Lr] Data última revisão:
171122
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170907
[St] Status:MEDLINE
[do] DOI:10.1056/NEJMoa1612665


  7 / 3189 MEDLINE  
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[PMID]:28797100
[Au] Autor:Tao Y; Fang P; Kim S; Guo M; Young NL; Marshall AG
[Ad] Endereço:Department of Chemistry and Biochemistry, Florida State University, Tallahassee, Florida, United States of America.
[Ti] Título:Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry.
[So] Source:PLoS One;12(8):e0181869, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Aminoacyl-tRNA synthetases-interacting multifunctional protein3 (AIMP3/p18) is involved in the macromolecular tRNA synthetase complex via its interaction with several aminoacyl-tRNA synthetases. Recent reports reveal a novel function of AIMP3 as a tumor suppressor by accelerating cellular senescence and causing defects in nuclear morphology. AIMP3 specifically mediates degradation of mature Lamin A (LmnA), a major component of the nuclear envelope matrix; however, the mechanism of how AIMP3 interacts with LmnA is unclear. Here we report solution-phase hydrogen/deuterium exchange (HDX) for AIMP3, LmnA, and AIMP3 in association with the LmnA C-terminus. Reversed-phase LC coupled with LTQ 14.5 T Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) results in high mass accuracy and resolving power for comparing the D-uptake profiles for AIMP3, LmnA, and their complex. The results show that the AIMP3-LmnA interaction involves one of the two putative binding sites and an adjacent novel interface on AIMP3. LmnA binds AIMP3 via its extreme C-terminus. Together these findings provide a structural insight for understanding the interaction between AIMP3 and LmnA in AIMP3 degradation.
[Mh] Termos MeSH primário: Lamina Tipo A/metabolismo
Fatores de Alongamento de Peptídeos/metabolismo
Proteínas Supressoras de Tumor/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Medição da Troca de Deutério/métodos
Seres Humanos
Lamina Tipo A/química
Espectrometria de Massas/métodos
Simulação de Acoplamento Molecular
Fatores de Alongamento de Peptídeos/química
Ligação Proteica
Mapeamento de Interação de Proteínas
Mapas de Interação de Proteínas
Proteólise
Proteínas Supressoras de Tumor/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (EEF1E1 protein, human); 0 (Lamin Type A); 0 (Peptide Elongation Factors); 0 (Tumor Suppressor Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170811
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181869


  8 / 3189 MEDLINE  
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[PMID]:28605514
[Au] Autor:Shi D; Svetlov D; Abagyan R; Artsimovitch I
[Ad] Endereço:Department of Chemistry and Biochemistry, University of California, San Diego, CA 92093, USA.
[Ti] Título:Flipping states: a few key residues decide the winning conformation of the only universally conserved transcription factor.
[So] Source:Nucleic Acids Res;45(15):8835-8843, 2017 Sep 06.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Transcription factors from the NusG family bind to the elongating RNA polymerase to enable synthesis of long RNAs in all domains of life. In bacteria, NusG frequently co-exists with specialized paralogs that regulate expression of a small set of targets, many of which encode virulence factors. Escherichia coli RfaH is the exemplar of this regulatory mechanism. In contrast to NusG, which freely binds to RNA polymerase, RfaH exists in a structurally distinct autoinhibitory state in which the RNA polymerase-binding site is buried at the interface between two RfaH domains. Binding to an ops DNA sequence triggers structural transformation wherein the domains dissociate and RfaH refolds into a NusG-like structure. Formation of the autoinhibitory state, and thus sequence-specific recruitment, represents the decisive step in the evolutionary history of the RfaH subfamily. We used computational and experimental approaches to identify the residues that confer the unique regulatory properties of RfaH. Our analysis highlighted highly conserved Ile and Phe residues at the RfaH interdomain interface. Replacement of these residues with equally conserved Glu and Val counterpart residues in NusG destabilized interactions between the RfaH domains and allowed sequence-independent recruitment to RNA polymerase, suggesting a plausible pathway for diversification of NusG paralogs.
[Mh] Termos MeSH primário: DNA Bacteriano/química
RNA Polimerases Dirigidas por DNA/química
Proteínas de Escherichia coli/química
Regulação Bacteriana da Expressão Gênica
Fatores de Alongamento de Peptídeos/química
Transativadores/química
Fatores de Transcrição/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Substituição de Aminoácidos
Sítios de Ligação
DNA Bacteriano/genética
DNA Bacteriano/metabolismo
RNA Polimerases Dirigidas por DNA/genética
RNA Polimerases Dirigidas por DNA/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Evolução Molecular
Ácido Glutâmico/química
Ácido Glutâmico/metabolismo
Isoleucina/química
Isoleucina/metabolismo
Modelos Moleculares
Fatores de Alongamento de Peptídeos/genética
Fatores de Alongamento de Peptídeos/metabolismo
Fenilalanina/química
Fenilalanina/metabolismo
Ligação Proteica
Dobramento de Proteína
Domínios e Motivos de Interação entre Proteínas
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Transativadores/genética
Transativadores/metabolismo
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Transcrição Genética
Valina/química
Valina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Escherichia coli Proteins); 0 (NusG protein, E coli); 0 (Peptide Elongation Factors); 0 (RfaH protein, E coli); 0 (Trans-Activators); 0 (Transcription Factors); 04Y7590D77 (Isoleucine); 3KX376GY7L (Glutamic Acid); 47E5O17Y3R (Phenylalanine); EC 2.7.7.6 (DNA-Directed RNA Polymerases); HG18B9YRS7 (Valine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170613
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx523


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[PMID]:28515276
[Au] Autor:Malinová A; Cvacková Z; Mateju D; Horejsí Z; Abéza C; Vandermoere F; Bertrand E; Stanek D; Verheggen C
[Ad] Endereço:Institute of Molecular Genetics, Czech Academy of Sciences, 142 20 Prague, Czech Republic.
[Ti] Título:Assembly of the U5 snRNP component PRPF8 is controlled by the HSP90/R2TP chaperones.
[So] Source:J Cell Biol;216(6):1579-1596, 2017 Jun 05.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Splicing is catalyzed by the spliceosome, a complex of five major small nuclear ribonucleoprotein particles (snRNPs). The pre-mRNA splicing factor PRPF8 is a crucial component of the U5 snRNP, and together with EFTUD2 and SNRNP200, it forms a central module of the spliceosome. Using quantitative proteomics, we identified assembly intermediates containing PRPF8, EFTUD2, and SNRNP200 in association with the HSP90/R2TP complex, its ZNHIT2 cofactor, and additional proteins. HSP90 and R2TP bind unassembled U5 proteins in the cytoplasm, stabilize them, and promote the formation of the U5 snRNP. We further found that PRPF8 mutants causing Retinitis pigmentosa assemble less efficiently with the U5 snRNP and bind more strongly to R2TP, with one mutant retained in the cytoplasm in an R2TP-dependent manner. We propose that the HSP90/R2TP chaperone system promotes the assembly of a key module of U5 snRNP while assuring the quality control of PRPF8. The proteomics data further reveal new interactions between R2TP and the tuberous sclerosis complex (TSC), pointing to a potential link between growth signals and the assembly of key cellular machines.
[Mh] Termos MeSH primário: Proteínas de Choque Térmico HSP90/metabolismo
Precursores de RNA/metabolismo
Processamento de RNA
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/metabolismo
Ribonucleoproteína Nuclear Pequena U5/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Ligação ao Cálcio/metabolismo
Células HeLa
Seres Humanos
Complexos Multiproteicos
Mutação
Fatores de Alongamento de Peptídeos/genética
Fatores de Alongamento de Peptídeos/metabolismo
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estabilidade Proteica
Proteômica/métodos
Interferência de RNA
Precursores de RNA/genética
RNA Mensageiro/genética
Proteínas de Ligação a RNA/genética
Retinite Pigmentosa/genética
Retinite Pigmentosa/metabolismo
Ribonucleoproteína Nuclear Pequena U1/metabolismo
Ribonucleoproteína Nuclear Pequena U4-U6/metabolismo
Ribonucleoproteína Nuclear Pequena U5/genética
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calcium-Binding Proteins); 0 (EFTUD2 protein, human); 0 (HSP90 Heat-Shock Proteins); 0 (Multiprotein Complexes); 0 (PRPF8 protein, human); 0 (Peptide Elongation Factors); 0 (RNA Precursors); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (Ribonucleoprotein, U1 Small Nuclear); 0 (Ribonucleoprotein, U4-U6 Small Nuclear); 0 (Ribonucleoprotein, U5 Small Nuclear); 0 (TSC protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170519
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201701165


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[PMID]:28472342
[Au] Autor:Jamar NH; Kritsiligkou P; Grant CM
[Ad] Endereço:The University of Manchester, Faculty of Biology, Medicine and Health, Manchester M13 9PT, UK.
[Ti] Título:The non-stop decay mRNA surveillance pathway is required for oxidative stress tolerance.
[So] Source:Nucleic Acids Res;45(11):6881-6893, 2017 Jun 20.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Reactive oxygen species (ROS) are toxic by-products of normal aerobic metabolism. ROS can damage mRNAs and the translational apparatus resulting in translational defects and aberrant protein production. Three mRNA quality control systems monitor mRNAs for translational errors: nonsense-mediated decay, non-stop decay (NSD) and no-go decay (NGD) pathways. Here, we show that factors required for the recognition of NSD substrates and components of the SKI complex are required for oxidant tolerance. We found an overlapping requirement for Ski7, which bridges the interaction between the SKI complex and the exosome, and NGD components (Dom34/Hbs1) which have been shown to function in both NSD and NGD. We show that ski7 dom34 and ski7 hbs1 mutants are sensitive to hydrogen peroxide stress and accumulate an NSD substrate. We further show that NSD substrates are generated during ROS exposure as a result of aggregation of the Sup35 translation termination factor, which increases stop codon read-through allowing ribosomes to translate into the 3΄-end of mRNAs. Overexpression of Sup35 decreases stop codon read-through and rescues oxidant tolerance consistent with this model. Our data reveal an unanticipated requirement for the NSD pathway during oxidative stress conditions which prevents the production of aberrant proteins from NSD mRNAs.
[Mh] Termos MeSH primário: Estresse Oxidativo
Estabilidade de RNA
RNA Fúngico/metabolismo
RNA Mensageiro/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Adaptação Fisiológica
Proteínas Adaptadoras de Transdução de Sinal/fisiologia
Proteínas de Ciclo Celular/fisiologia
Endorribonucleases/fisiologia
Proteínas de Ligação ao GTP/fisiologia
Regulação Fúngica da Expressão Gênica
Proteínas de Choque Térmico HSP70/fisiologia
Viabilidade Microbiana
Fatores de Alongamento de Peptídeos/fisiologia
Fatores de Terminação de Peptídeos/genética
Fatores de Terminação de Peptídeos/metabolismo
Biossíntese de Proteínas
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Cell Cycle Proteins); 0 (HBS1 protein, S cerevisiae); 0 (HSP70 Heat-Shock Proteins); 0 (Peptide Elongation Factors); 0 (Peptide Termination Factors); 0 (RNA, Fungal); 0 (RNA, Messenger); 0 (SKI2 protein, S cerevisiae); 0 (SKI7 protein, S cerevisiae); 0 (SUP35 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); EC 3.1.- (Dom34 protein, S cerevisiae); EC 3.1.- (Endoribonucleases); EC 3.6.1.- (GTP-Binding Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx306



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