Base de dados : MEDLINE
Pesquisa : D12.644.360.175 [Categoria DeCS]
Referências encontradas : 145 [refinar]
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[PMID]:29307824
[Au] Autor:Yan J; He H; Fang L; Zhang A
[Ad] Endereço:National Key Laboratory of Crop Genetics and Germplasm Enhancement, Nanjing Agricultural University, Nanjing, Jiangsu, 210095, China; College of Life Sciences, Nanjing Agricultural University, Nanjing, Jiangsu, 210095, China.
[Ti] Título:Pectin methylesterase31 positively regulates salt stress tolerance in Arabidopsis.
[So] Source:Biochem Biophys Res Commun;496(2):497-501, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The alteration of cell wall component and structure is an important adaption to saline environment. Pectins, a major cell wall component, are often present in a highly methylesterified form. The level of methyl esterification determined by pectin methylesterases (PMEs) influences many important wall properties that are believed to relate to the adaption to saline stress. However, little is known about the function of PMEs in response to salt stress. Here, we established a link between pectin methylesterase31 (PME31) and salt stress tolerance. Salt stress significantly increases PME31 expression. PME31 is located in the plasma membrane and the expression level of PME31 was high in dry seeds. Knock-down mutants in PME31 conferred hypersensitive phenotypes to salt stress in seed germination and post-germination growth. Real-time PCR analysis revealed that the transcript levels of several stress genes (DREB2A, RD29A and RD29B) are lower in pme31-2 mutant than that in the wild type in response to salt stress. These results suggested that PME31 could positively modulate salt stress tolerance.
[Mh] Termos MeSH primário: Arabidopsis/efeitos dos fármacos
Hidrolases de Éster Carboxílico/genética
Regulação da Expressão Gênica de Plantas
Células Vegetais/efeitos dos fármacos
Cloreto de Sódio/farmacologia
[Mh] Termos MeSH secundário: Arabidopsis/genética
Arabidopsis/metabolismo
Proteínas de Arabidopsis/genética
Proteínas de Arabidopsis/metabolismo
Hidrolases de Éster Carboxílico/metabolismo
Membrana Celular/efeitos dos fármacos
Membrana Celular/metabolismo
Parede Celular/efeitos dos fármacos
Parede Celular/metabolismo
Proteínas e Peptídeos de Choque Frio/genética
Proteínas e Peptídeos de Choque Frio/metabolismo
Germinação/efeitos dos fármacos
Isoenzimas/genética
Isoenzimas/metabolismo
Mutação
Células Vegetais/metabolismo
Salinidade
Tolerância a Sal
Sementes/efeitos dos fármacos
Sementes/genética
Sementes/metabolismo
Estresse Fisiológico
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Cold Shock Proteins and Peptides); 0 (DREB2A protein, Arabidopsis); 0 (Isoenzymes); 0 (RD29B protein, Arabidopsis); 0 (RD29a protein, Arabidopsis); 0 (Transcription Factors); 451W47IQ8X (Sodium Chloride); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.11 (pectinesterase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


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[PMID]:29175331
[Au] Autor:Fujita T; Liu Y; Higashitsuji H; Itoh K; Shibasaki K; Fujita J; Nishiyama H
[Ad] Endereço:Department of Urology, Faculty of Medicine, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8575, Japan; Department of Clinical Molecular Biology, Graduate School of Medicine, Kyoto University, 54 Shogoin Kawahara-cho, Sakyo-ku, Kyoto 606-8507, Japan.
[Ti] Título:Involvement of TRPV3 and TRPM8 ion channel proteins in induction of mammalian cold-inducible proteins.
[So] Source:Biochem Biophys Res Commun;495(1):935-940, 2018 01 01.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cold-inducible RNA-binding protein (CIRP), RNA-binding motif protein 3 (RBM3) and serine and arginine rich splicing factor 5 (SRSF5) are RNA-binding proteins that are transcriptionally upregulated in response to moderately low temperatures and a variety of cellular stresses in mammalian cells. Induction of these cold-inducible proteins (CIPs) is dependent on transient receptor potential (TRP) V4 channel protein, but seems independent of its ion channel activity. We herein report that in addition to TRPV4, TRPV3 and TRPM8 are necessary for the induction of CIPs. We established cell lines from the lung of TRPV4-knockout (KO) mouse, and observed induction of CIPs in them by western blot analysis. A TRPV4 antagonist RN1734 suppressed the induction in wild-type mouse cells, but not in TRPV4-KO cells. A TRPV3 channel blocker S408271 and a TRPM8 channel blocker AMTB as well as siRNAs against TRPV3 and TRPM8 suppressed the CIP induction in mouse TRPV4-KO cells and human U-2 OS cells. A TRPV3 channel agonist 2-APB induced CIP expression, but camphor did not. Neither did a TRPM8 channel agonist WS-12. These results suggest that TRPV4, TRPV3 and TRPM8 proteins, but not their ion channel activities are necessary for the induction of CIPs at 32 °C. Identification of proteins that differentially interact with these TRP channels at 37 °C and 32 °C would help elucidate the underlying mechanisms of CIP induction by hypothermia.
[Mh] Termos MeSH primário: Proteínas e Peptídeos de Choque Frio/metabolismo
Resposta ao Choque Frio/fisiologia
Ativação do Canal Iônico/fisiologia
Canais de Cátion TRPM/metabolismo
Canais de Cátion TRPV/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Temperatura Baixa
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cold Shock Proteins and Peptides); 0 (TRPM Cation Channels); 0 (TRPM8 protein, mouse); 0 (TRPV Cation Channels); 0 (Trpv3 protein, mouse); 0 (Trpv4 protein, mouse)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE


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[PMID]:28126922
[Au] Autor:Rennella E; Sára T; Juen M; Wunderlich C; Imbert L; Solyom Z; Favier A; Ayala I; Weinhäupl K; Schanda P; Konrat R; Kreutz C; Brutscher B
[Ad] Endereço:Institut de Biologie Structurale, Université Grenoble 1, 71 avenue des Martyrs, 38044 Grenoble Cedex 9, France.
[Ti] Título:RNA binding and chaperone activity of the E. coli cold-shock protein CspA.
[So] Source:Nucleic Acids Res;45(7):4255-4268, 2017 Apr 20.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ensuring the correct folding of RNA molecules in the cell is of major importance for a large variety of biological functions. Therefore, chaperone proteins that assist RNA in adopting their functionally active states are abundant in all living organisms. An important feature of RNA chaperone proteins is that they do not require an external energy source to perform their activity, and that they interact transiently and non-specifically with their RNA targets. So far, little is known about the mechanistic details of the RNA chaperone activity of these proteins. Prominent examples of RNA chaperones are bacterial cold shock proteins (Csp) that have been reported to bind single-stranded RNA and DNA. Here, we have used advanced NMR spectroscopy techniques to investigate at atomic resolution the RNA-melting activity of CspA, the major cold shock protein of Escherichia coli, upon binding to different RNA hairpins. Real-time NMR provides detailed information on the folding kinetics and folding pathways. Finally, comparison of wild-type CspA with single-point mutants and small peptides yields insights into the complementary roles of aromatic and positively charged amino-acid side chains for the RNA chaperone activity of the protein.
[Mh] Termos MeSH primário: Proteínas e Peptídeos de Choque Frio/química
Proteínas e Peptídeos de Choque Frio/metabolismo
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/metabolismo
Dobramento de RNA
RNA/química
[Mh] Termos MeSH secundário: Aminoácidos Aromáticos/química
Ressonância Magnética Nuclear Biomolecular
Conformação de Ácido Nucleico
Ligação Proteica
Conformação Proteica
RNA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids, Aromatic); 0 (Cold Shock Proteins and Peptides); 0 (CspA protein, E coli); 0 (Escherichia coli Proteins); 63231-63-0 (RNA)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170128
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx044


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[PMID]:27770200
[Au] Autor:Seok HY; Woo DH; Nguyen LV; Tran HT; Tarte VN; Mehdi SM; Lee SY; Moon YH
[Ad] Endereço:Department of Molecular Biology, Pusan National University, Busan, 609-735, South Korea.
[Ti] Título:Arabidopsis AtNAP functions as a negative regulator via repression of AREB1 in salt stress response.
[So] Source:Planta;245(2):329-341, 2017 Feb.
[Is] ISSN:1432-2048
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:MAIN CONCLUSION: AtNAP , an Arabidopsis NAC transcription factor family gene, functions as a negative regulator via transcriptional repression of AREB1 in salt stress response. AtNAP is an NAC family transcription factor in Arabidopsis and is known to be a positive regulator of senescence. However, its exact function and underlying molecular mechanism in stress responses are not well known. Here, we investigated functional roles of AtNAP in salt stress response. AtNAP expression significantly increased at the seedling stage, with higher expression in both shoots and roots under NaCl, mannitol, and ABA treatments. T-DNA insertional loss-of-function mutants of AtNAP were more tolerant to salt stress than wild type (WT), whereas AtNAP-overexpressing transgenic plants (OXs) were more sensitive to salt stress than WT during germination, seedling development, and mature plant stage. Transcript levels of stress-responsive genes in the ABA-dependent pathway, such as AREB1, RD20, and RD29B, were significantly higher and lower in atnap mutants and AtNAP OXs, respectively, than in WT under salt stress conditions, suggesting that AtNAP might negatively regulate the expression of those genes under salt stress conditions. Indeed, AtNAP repressed the promoter activity of AREB1 under normal and salt stress conditions. These results indicate that AtNAP functions as a negative regulator in the salt stress response. Our results, together with previous studies, suggest that AtNAP functions as a negative regulator in osmotic stress responses, whereas it functions as a positive regulator in senescence.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/fisiologia
Fatores de Transcrição de Zíper de Leucina Básica/metabolismo
Estresse Fisiológico/genética
[Mh] Termos MeSH secundário: Arabidopsis/efeitos dos fármacos
Proteínas de Arabidopsis/genética
Fatores de Transcrição de Zíper de Leucina Básica/genética
Proteínas de Ligação ao Cálcio/genética
Proteínas de Ligação ao Cálcio/metabolismo
Proteínas e Peptídeos de Choque Frio/genética
Proteínas e Peptídeos de Choque Frio/metabolismo
Regulação da Expressão Gênica de Plantas
Pressão Osmótica
Plantas Geneticamente Modificadas
Regiões Promotoras Genéticas
Plântulas/genética
Plântulas/crescimento & desenvolvimento
Cloreto de Sódio/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AREB1 protein, Arabidopsis); 0 (Arabidopsis Proteins); 0 (Basic-Leucine Zipper Transcription Factors); 0 (Calcium-Binding Proteins); 0 (Cold Shock Proteins and Peptides); 0 (NAP protein, Arabidopsis); 0 (RD20 protein, Arabidopsis); 0 (RD29B protein, Arabidopsis); 451W47IQ8X (Sodium Chloride)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE
[do] DOI:10.1007/s00425-016-2609-0


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[PMID]:27750393
[Au] Autor:Koh HY; Park H; Lee JH; Han SJ; Sohn YC; Lee SG
[Ad] Endereço:Unit of Polar Genomics Korea Polar Research Institute, Incheon, South Korea.
[Ti] Título:Proteomic and transcriptomic investigations on cold-responsive properties of the psychrophilic Antarctic bacterium Psychrobacter sp. PAMC 21119 at subzero temperatures.
[So] Source:Environ Microbiol;19(2):628-644, 2017 Feb.
[Is] ISSN:1462-2920
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Psychrobacter sp. PAMC 21119, isolated from Antarctic permafrost soil, grows and proliferates at subzero temperatures. However, its major mechanism of cold adaptation regulation remains poorly understood. We investigated the transcriptomic and proteomic responses of this species to cold temperatures by comparing profiles at -5°C and 20°C to understand how extreme microorganisms survive under subzero conditions. We found a total of 2,906 transcripts and 584 differentially expressed genes (≥ twofold, P <0.005) by RNA-seq. Genes for translation, ribosomal structure and biogenesis were upregulated, and lipid transport and metabolism was downregulated at low temperatures. A total of 60 protein spots (≥ 1.8 fold, P < 0.005) showed differential expression on two-dimensional gel electrophoresis and the proteins were identified by mass spectrometry. The most prominent upregulated proteins in response to cold were involved in metabolite transport, protein folding and membrane fluidity. Proteins involved in energy production and conversion, and heme protein synthesis were downregulated. Moreover, isoform exchange of cold-shock proteins was detected at both temperatures. Interestingly, pathways for acetyl-CoA metabolism, putrescine synthesis and amino acid metabolism were upregulated. This study highlights some of the strategies and different physiological states that Psychrobacter sp. PAMC 21119 has developed to adapt to the cold environment in Antarctica.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Proteínas e Peptídeos de Choque Frio/metabolismo
Temperatura Baixa
Proteômica
Psychrobacter/fisiologia
Transcriptoma
[Mh] Termos MeSH secundário: Acetilcoenzima A/metabolismo
Regiões Antárticas
Proteínas de Bactérias/genética
Proteínas e Peptídeos de Choque Frio/genética
Regulação Bacteriana da Expressão Gênica
Dobramento de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cold Shock Proteins and Peptides); 72-89-9 (Acetyl Coenzyme A)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161018
[St] Status:MEDLINE
[do] DOI:10.1111/1462-2920.13578


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[PMID]:26995407
[Au] Autor:Wu L; Sun HL; Gao Y; Hui KL; Xu MM; Zhong H; Duan ML
[Ad] Endereço:Department of Anesthesiology, Jinling Hospital, School of Medicine, Nanjing University, Nanjing, 210002, China.
[Ti] Título:Therapeutic Hypothermia Enhances Cold-Inducible RNA-Binding Protein Expression and Inhibits Mitochondrial Apoptosis in a Rat Model of Cardiac Arrest.
[So] Source:Mol Neurobiol;54(4):2697-2705, 2017 05.
[Is] ISSN:1559-1182
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Therapeutic hypothermia is well known for its protective effect against brain injury after cardiac arrest, but the exact mechanism remains unclear. Cold-inducible RNA-binding protein (CIRP), a member of cold shock protein, enables mammalian cells to withstand decreased temperature by regulating gene translation. However, the role of CIRP in global cerebral ischemia after therapeutic hypothermia has not been clearly elucidated. In the present study, rats resuscitated from 4 min of cardiac arrest were separately treated with therapeutic hypothermia (immediately after return of spontaneous circulation (ROSC); targeted temperature at 33 °C) and therapeutic normothermia (targeted temperature at 36.8 °C) for 6 h. The hippocampus was harvested at 0 h (baseline), 6 h, 12 h, 1 day, 3 days, and 7 days after ROSC. The expression of CIRP messenger RNA (mRNA) was assessed by real-time PCR. CIRP and mitochondrial apoptosis-associated proteins were tested by Western blot. The histological changes and neurological function were respectively evaluated by hematoxylin-eosin staining and neurological deficit score (NDS). Compared with baseline, rats resuscitated from cardiac arrest showed increased expression of CIRP, Bax, Caspase 9, and Caspase 3 and decreased expression of Bcl-2 in hippocampus (P < 0.05). However, therapeutic hypothermia after ROSC alleviated the alterations of Bax, Caspase 9, Caspase 3, and Bcl-2, while further increased the hippocampal expression of CIRP mRNA and protein, when compared with the normothermia rats (P < 0.05). In addition, compared with the therapeutic normothermia rats, histopathological damage in CA1 zone and NDS were respectively decreased and increased in the hypothermia rats (P < 0.05). Our findings suggest that 32 °C therapeutic hypothermia exerts an important neuroprotective effects by up-regulating CIRP expression and inhibiting mitochondrial apoptosis factor production in the cardiac arrest rat model.
[Mh] Termos MeSH primário: Apoptose
Proteínas e Peptídeos de Choque Frio/metabolismo
Parada Cardíaca/metabolismo
Parada Cardíaca/patologia
Hipotermia Induzida
Mitocôndrias/metabolismo
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Animais
Caspase 3/metabolismo
Caspase 9/metabolismo
Modelos Animais de Doenças
Hipocampo/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Ratos Sprague-Dawley
Análise de Sobrevida
Proteína X Associada a bcl-2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cirp protein, rat); 0 (Cold Shock Proteins and Peptides); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (bcl-2-Associated X Protein); EC 3.4.22.- (Caspase 3); EC 3.4.22.- (Caspase 9)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171120
[Lr] Data última revisão:
171120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160321
[St] Status:MEDLINE
[do] DOI:10.1007/s12035-016-9813-6


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[PMID]:27556928
[Au] Autor:Larrayoz IM; Rey-Funes M; Contartese DS; Rolón F; Sarotto A; Dorfman VB; Loidl CF; Martínez A
[Ad] Endereço:Angiogenesis Study Group, Center for Biomedical Research of La Rioja (CIBIR), 26006, Logroño, Spain.
[Ti] Título:Cold Shock Proteins Are Expressed in the Retina Following Exposure to Low Temperatures.
[So] Source:PLoS One;11(8):e0161458, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hypothermia has been proposed as a therapeutic intervention for some retinal conditions, including ischemic insults. Cold exposure elevates expression of cold-shock proteins (CSP), including RNA-binding motif protein 3 (RBM3) and cold inducible RNA-binding protein (CIRP), but their presence in mammalian retina is so far unknown. Here we show the effects of hypothermia on the expression of these CSPs in retina-derived cell lines and in the retina of newborn and adult rats. Two cell lines of retinal origin, R28 and mRPE, were exposed to 32°C for different time periods and CSP expression was measured by qRT-PCR and Western blotting. Neonatal and adult Sprague-Dawley rats were exposed to a cold environment (8°C) and expression of CSPs in their retinas was studied by Western blotting, multiple inmunofluorescence, and confocal microscopy. RBM3 expression was upregulated by cold in both R28 and mRPE cells in a time-dependent fashion. On the other hand, CIRP was upregulated in R28 cells but not in mRPE. In vivo, expression of CSPs was negligible in the retina of newborn and adult rats kept at room temperature (24°C). Exposure to a cold environment elicited a strong expression of both proteins, especially in retinal pigment epithelium cells, photoreceptors, bipolar, amacrine and horizontal cells, Müller cells, and ganglion cells. In conclusion, CSP expression rapidly rises in the mammalian retina following exposure to hypothermia in a cell type-specific pattern. This observation may be at the basis of the molecular mechanism by which hypothermia exerts its therapeutic effects in the retina.
[Mh] Termos MeSH primário: Proteínas e Peptídeos de Choque Frio/genética
Temperatura Baixa
Expressão Gênica
Hipotermia/genética
Retina/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Biomarcadores
Proteínas de Transporte
Proteínas e Peptídeos de Choque Frio/metabolismo
Exposição Ambiental
Hipotermia/metabolismo
Macaca mulatta
Masculino
Ligação Proteica
Transporte Proteico
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Carrier Proteins); 0 (Cold Shock Proteins and Peptides)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160825
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0161458


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[PMID]:27524241
[Au] Autor:Rauen T; Frye BC; Wang J; Raffetseder U; Alidousty C; En-Nia A; Floege J; Mertens PR
[Ad] Endereço:Nephrology and Clinical Immunology, RWTH University of Aachen, Aachen, Germany.
[Ti] Título:Cold shock protein YB-1 is involved in hypoxia-dependent gene transcription.
[So] Source:Biochem Biophys Res Commun;478(2):982-7, 2016 09 16.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hypoxia-dependent gene regulation is largely orchestrated by hypoxia-inducible factors (HIFs), which associate with defined nucleotide sequences of hypoxia-responsive elements (HREs). Comparison of the regulatory HRE within the 3' enhancer of the human erythropoietin (EPO) gene with known binding motifs for cold shock protein Y-box (YB) protein-1 yielded strong similarities within the Y-box element and 3' adjacent sequences. DNA binding assays confirmed YB-1 binding to both, single- and double-stranded HRE templates. Under hypoxia, we observed nuclear shuttling of YB-1 and co-immunoprecipitation assays demonstrated that YB-1 and HIF-1α physically interact with each other. Cellular YB-1 depletion using siRNA significantly induced hypoxia-dependent EPO production at both, promoter and mRNA level. Vice versa, overexpressed YB-1 significantly reduced EPO-HRE-dependent gene transcription, whereas this effect was minor under normoxia. HIF-1α overexpression induced hypoxia-dependent gene transcription through the same element and accordingly, co-expression with YB-1 reduced HIF-1α-mediated EPO induction under hypoxic conditions. Taken together, we identified YB-1 as a novel binding factor for HREs that participates in fine-tuning of the hypoxia transcriptome.
[Mh] Termos MeSH primário: Proteínas e Peptídeos de Choque Frio/metabolismo
Transcrição Genética
Proteína 1 de Ligação a Y-Box/metabolismo
[Mh] Termos MeSH secundário: Sequência de Bases
Sítios de Ligação
Hipóxia Celular/genética
Núcleo Celular/metabolismo
Regulação da Expressão Gênica
Células HEK293
Células HeLa
Células Hep G2
Seres Humanos
Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo
Ligação Proteica/genética
Transporte Proteico
Elementos de Resposta/genética
Análise de Sequência de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cold Shock Proteins and Peptides); 0 (Hypoxia-Inducible Factor 1, alpha Subunit); 0 (Y-Box-Binding Protein 1)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171127
[Lr] Data última revisão:
171127
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160816
[St] Status:MEDLINE


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[PMID]:27477251
[Au] Autor:Porter T; Frederick D; Johnson E; Jones PG
[Ad] Endereço:Department of Biological Sciences, Winston-Salem State University.
[Ti] Título:A requirement for cell elongation protein RodZ and cell division proteins FtsN and DedD to maintain the small rod morphology of Escherichia coli at growth temperatures near 8°C.
[So] Source:J Gen Appl Microbiol;62(4):189-98, 2016 Sep 12.
[Is] ISSN:1349-8037
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:As similarly observed in nutrient-poor media at 37°C, Escherichia coli forms small rods in nutrient-rich media at temperatures near 8°C, the minimum temperature of growth. A study was initiated to identify proteins required to facilitate the small rod morphology at low temperature. E. coli contains three nonessential SPOR domain proteins (DamX, RlpA, and DedD) that have been demonstrated to bind to the septal ring. In contrast to the normal growth and small rod morphology of damX and rlpA null mutants at 10°C, the dedD null mutant exhibited reduced growth and formed filamentous cells. The presence of plasmid-encoded DedD restored growth and small rods. Plasmid-encoded FtsN, an essential SPOR domain protein that functions to stabilize the septal ring and to initiate septation, in the dedD null mutant resulted in increased growth and the formation of shorter chained cells. However, plasmid-encoded DedD failed to restore growth and cell division of cells lacking FtsN at 10°C. In contrast to cell division protein DedD, RodZ is a cell elongation protein particularly required for growth at 30°C. However, the rodZ null mutant grew similarly as the wild type strain and produced cocci in LB broth at 10°C. Moreover at 10°C, the concerted deletion of dedD and rodZ resulted in severe inhibition of growth accompanied with the formation of swollen prolate ellipsoids due to a block in septal ring assembly and cell elongation. The data indicate the cellular requirement of both FtsN and DedD for septation as well as RodZ for cell elongation to maintain the small rod morphology at temperatures near 8°C. In comparison to the growth and small rods of the wild type in M9-glucose minimal media at 37°C, the dedD null mutant grew at the same rate and produced elongated cells while the rodZ null mutant grew at a slightly slower rate and produced cocci. The data indicate that DedD and RodZ are also required to maintain the small rod morphology in nutrient-poor media, but there is a higher cellular requirement of DedD for growth and cell division in nutrient-rich media at low temperature.
[Mh] Termos MeSH primário: Temperatura Baixa
Proteínas do Citoesqueleto/metabolismo
Proteínas de Escherichia coli/metabolismo
Escherichia coli/citologia
Escherichia coli/metabolismo
Proteínas de Membrana/metabolismo
[Mh] Termos MeSH secundário: Divisão Celular/genética
Proteínas e Peptídeos de Choque Frio/genética
Proteínas e Peptídeos de Choque Frio/metabolismo
Meios de Cultura/química
Proteínas do Citoesqueleto/genética
Escherichia coli/genética
Escherichia coli/crescimento & desenvolvimento
Proteínas de Escherichia coli/genética
Proteínas de Membrana/genética
Mutação
Plasmídeos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cold Shock Proteins and Peptides); 0 (Culture Media); 0 (Cytoskeletal Proteins); 0 (DedD protein, E coli); 0 (Escherichia coli Proteins); 0 (FtsN protein, E coli); 0 (Membrane Proteins); 0 (RodZ protein, E coli)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170412
[Lr] Data última revisão:
170412
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160802
[St] Status:MEDLINE
[do] DOI:10.2323/jgam.2016.02.006


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[PMID]:27338368
[Au] Autor:Zhou Y; Sun X; Yang Y; Li X; Cheng Y; Yang Y
[Ad] Endereço:Key Laboratory for Plant Diversity and Biogeography of East Asia, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming 650201, China. zhouyanli@mail.kib.ac.cn.
[Ti] Título:Expression of Stipa purpurea SpCIPK26 in Arabidopsis thaliana Enhances Salt and Drought Tolerance and Regulates Abscisic Acid Signaling.
[So] Source:Int J Mol Sci;17(6), 2016 Jun 22.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Stipa purpurea (S. purpurea) is the dominant plant species in the alpine steppe of the Qinghai-Tibet Plateau, China. It is highly resistant to cold and drought conditions. However, the underlying mechanisms regulating the stress tolerance are unknown. In this study, a CIPK gene from S. purpurea (SpCIPK26) was isolated. The SpCIPK26 coding region consisted of 1392 bp that encoded 464 amino acids. The protein has a highly conserved catalytic structure and regulatory domain. The expression of SpCIPK26 was induced by drought and salt stress. SpCIPK26 overexpression in Arabidopsis thaliana (A. thaliana) plants provided increased tolerance to drought and salt stress in an abscisic acid (ABA)-dependent manner. Compared with wild-type A. thaliana plants, SpCIPK26-overexpressing plants had higher survival rates, water potentials, and photosynthetic efficiency (Fv/Fm), as well as lower levels of reactive oxygen species (ROS) following exposure to drought and salt stress. Gene expression analyses indicated stress-inducible genes (RD29A, RD29B, and ABF2) and a ROS-scavenger gene (CAT1) were upregulated in SpCIPK26-overexpressing plants after stress treatments. All of these marker genes are associated with ABA-responsive cis-acting elements. Additionally, the similarities in the gene expression patterns following ABA, mannitol, and NaCl treatments suggest SpCIPK26 has an important role during plant responses to drought and salt stress and in regulating ABA signaling.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/genética
Arabidopsis/genética
Proteínas Quinases/genética
Tolerância a Sal/genética
Estresse Fisiológico
Transgenes
[Mh] Termos MeSH secundário: Arabidopsis/metabolismo
Proteínas de Arabidopsis/química
Proteínas de Arabidopsis/metabolismo
Catalase/genética
Catalase/metabolismo
Proteínas e Peptídeos de Choque Frio/genética
Proteínas e Peptídeos de Choque Frio/metabolismo
Sequência Conservada
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/metabolismo
Secas
Regulação da Expressão Gênica de Plantas
Poaceae/genética
Domínios Proteicos
Proteínas Quinases/química
Proteínas Quinases/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABF2 protein, Arabidopsis); 0 (Arabidopsis Proteins); 0 (Cold Shock Proteins and Peptides); 0 (DNA-Binding Proteins); 0 (RD29B protein, Arabidopsis); 0 (RD29a protein, Arabidopsis); 0 (Reactive Oxygen Species); 0 (Transcription Factors); EC 1.11.1.6 (Catalase); EC 2.7.- (CIPK26 protein, Arabidopsis); EC 2.7.- (Protein Kinases)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170315
[Lr] Data última revisão:
170315
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160625
[St] Status:MEDLINE



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