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[PMID]:28723971
[Au] Autor:Bidnenko V; Nicolas P; Grylak-Mielnicka A; Delumeau O; Auger S; Aucouturier A; Guerin C; Repoila F; Bardowski J; Aymerich S; Bidnenko E
[Ad] Endereço:Micalis Institute, INRA, AgroParisTech, Université Paris-Saclay, Jouy-en-Josas, France.
[Ti] Título:Termination factor Rho: From the control of pervasive transcription to cell fate determination in Bacillus subtilis.
[So] Source:PLoS Genet;13(7):e1006909, 2017 Jul.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In eukaryotes, RNA species originating from pervasive transcription are regulators of various cellular processes, from the expression of individual genes to the control of cellular development and oncogenesis. In prokaryotes, the function of pervasive transcription and its output on cell physiology is still unknown. Most bacteria possess termination factor Rho, which represses pervasive, mostly antisense, transcription. Here, we investigate the biological significance of Rho-controlled transcription in the Gram-positive model bacterium Bacillus subtilis. Rho inactivation strongly affected gene expression in B. subtilis, as assessed by transcriptome and proteome analysis of a rho-null mutant during exponential growth in rich medium. Subsequent physiological analyses demonstrated that a considerable part of Rho-controlled transcription is connected to balanced regulation of three mutually exclusive differentiation programs: cell motility, biofilm formation, and sporulation. In the absence of Rho, several up-regulated sense and antisense transcripts affect key structural and regulatory elements of these differentiation programs, thereby suppressing motility and biofilm formation and stimulating sporulation. We dissected how Rho is involved in the activity of the cell fate decision-making network, centered on the master regulator Spo0A. We also revealed a novel regulatory mechanism of Spo0A activation through Rho-dependent intragenic transcription termination of the protein kinase kinB gene. Altogether, our findings indicate that distinct Rho-controlled transcripts are functional and constitute a previously unknown built-in module for the control of cell differentiation in B. subtilis. In a broader context, our results highlight the recruitment of the termination factor Rho, for which the conserved biological role is probably to repress pervasive transcription, in highly integrated, bacterium-specific, regulatory networks.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Fator Rho/genética
Fatores de Transcrição/genética
Terminação da Transcrição Genética
Transcrição Genética
[Mh] Termos MeSH secundário: Bacillus subtilis/genética
Biofilmes/crescimento & desenvolvimento
Movimento Celular/genética
Regulação Bacteriana da Expressão Gênica
Redes Reguladoras de Genes/genética
Regiões Promotoras Genéticas
Esporos Bacterianos/genética
Transcriptoma/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Rho Factor); 0 (Spo0A protein, Bacillus subtilis); 0 (Transcription Factors)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170822
[Lr] Data última revisão:
170822
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170721
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006909


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[PMID]:28520932
[Au] Autor:Bastet L; Chauvier A; Singh N; Lussier A; Lamontagne AM; Prévost K; Massé E; Wade JT; Lafontaine DA
[Ad] Endereço:Department of Biology, Faculty of Sciences, RNA Group, Université de Sherbrooke, Sherbrooke, Quebec J1K 2R1, Canada.
[Ti] Título:Translational control and Rho-dependent transcription termination are intimately linked in riboswitch regulation.
[So] Source:Nucleic Acids Res;45(12):7474-7486, 2017 Jul 07.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Riboswitches are regulatory elements that control gene expression by altering RNA structure upon the binding of specific metabolites. Although Bacillus subtilis riboswitches have been shown to control premature transcription termination, less is known about regulatory mechanisms employed by Escherichia coli riboswitches, which are predicted to regulate mostly at the level of translation initiation. Here, we present experimental evidence suggesting that the majority of known E. coli riboswitches control transcription termination by using the Rho transcription factor. In the case of the thiamin pyrophosphate-dependent thiM riboswitch, we find that Rho-dependent transcription termination is triggered as a consequence of translation repression. Using in vitro and in vivo assays, we show that the Rho-mediated regulation relies on RNA target elements located at the beginning of thiM coding region. Gene reporter assays indicate that relocating Rho target elements to a different gene induces transcription termination, demonstrating that such elements are modular domains controlling Rho. Our work provides strong evidence that translationally regulating riboswitches also regulate mRNA levels through an indirect control mechanism ensuring tight control of gene expression.
[Mh] Termos MeSH primário: Escherichia coli/genética
Regulação Bacteriana da Expressão Gênica
Biossíntese de Proteínas
Fator Rho/genética
Riboswitch
Terminação da Transcrição Genética
[Mh] Termos MeSH secundário: Sequência de Bases
Escherichia coli/metabolismo
Genes Reporter
Conformação de Ácido Nucleico
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Fator Rho/metabolismo
Tiamina Pirofosfato/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Fusion Proteins); 0 (Rho Factor); 0 (Riboswitch); Q57971654Y (Thiamine Pyrophosphate)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170519
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx434


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[PMID]:28285914
[Au] Autor:Hutchings KM; Lisabeth EM; Rajeswaran W; Wilson MW; Sorenson RJ; Campbell PL; Ruth JH; Amin A; Tsou PS; Leipprandt JR; Olson SR; Wen B; Zhao T; Sun D; Khanna D; Fox DA; Neubig RR; Larsen SD
[Ad] Endereço:Vahlteich Medicinal Chemistry Core, College of Pharmacy, University of Michigan, Ann Arbor, MI 48109, USA.
[Ti] Título:Pharmacokinetic optimitzation of CCG-203971: Novel inhibitors of the Rho/MRTF/SRF transcriptional pathway as potential antifibrotic therapeutics for systemic scleroderma.
[So] Source:Bioorg Med Chem Lett;27(8):1744-1749, 2017 04 15.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We recently reported the development of a novel inhibitor of Rho-mediated gene transcription (1, CCG-203971) that is efficacious in multiple animal models of acute fibrosis, including scleroderma, when given intraperitoneally. The modest in vivo potency and poor pharmacokinetics (PK) of this lead, however, make it unsuitable for long term efficacy studies. We therefore undertook a systematic medicinal chemistry effort to improve both the metabolic stability and the solubility of 1, resulting in the identification of two analogs achieving over 10-fold increases in plasma exposures in mice. We subsequently showed that one of these analogs (8f, CCG-232601) could inhibit the development of bleomycin-induced dermal fibrosis in mice when administered orally at 50mg/kg, an effect that was comparable to what we had observed earlier with 1 at a 4-fold higher IP dose.
[Mh] Termos MeSH primário: Ácidos Nipecóticos/farmacocinética
Ácidos Nipecóticos/uso terapêutico
Fator Rho/antagonistas & inibidores
Escleroderma Sistêmico/tratamento farmacológico
Pele/efeitos dos fármacos
Ativação Transcricional/efeitos dos fármacos
[Mh] Termos MeSH secundário: Administração Oral
Animais
Modelos Animais de Doenças
Fibrose
Células HEK293
Seres Humanos
Camundongos
Ácidos Nipecóticos/administração & dosagem
Ácidos Nipecóticos/química
Fator Rho/metabolismo
Escleroderma Sistêmico/genética
Escleroderma Sistêmico/metabolismo
Escleroderma Sistêmico/patologia
Elemento de Resposta Sérica/efeitos dos fármacos
Pele/metabolismo
Pele/patologia
Transativadores/antagonistas & inibidores
Transativadores/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (MKL1 protein, human); 0 (N-(4-chlorophenyl)-1-((3-(furan-2-yl)phenyl)carbonyl)piperidine-3-carboxamide); 0 (Nipecotic Acids); 0 (Rho Factor); 0 (Trans-Activators)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170314
[St] Status:MEDLINE


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[PMID]:28123036
[Au] Autor:Kriner MA; Groisman EA
[Ad] Endereço:Department of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT 06536, USA.
[Ti] Título:RNA secondary structures regulate three steps of Rho-dependent transcription termination within a bacterial mRNA leader.
[So] Source:Nucleic Acids Res;45(2):631-642, 2017 Jan 25.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Transcription termination events in bacteria often require the RNA helicase Rho. Typically, Rho promotes termination at the end of coding sequences, but it can also terminate transcription within leader regions to implement regulatory decisions. Rho-dependent termination requires initial recognition of a Rho utilization (rut) site on a nascent RNA by Rho's primary binding surface. However, it is presently unclear what factors determine the location of transcription termination, how RNA secondary structures influence this process and whether mechanistic differences distinguish constitutive from regulated Rho-dependent terminators. We previously demonstrated that the 5' leader mRNA of the Salmonella corA gene can adopt two mutually exclusive conformations that dictate accessibility of a rut site to Rho. We now report that the corA leader also controls two subsequent steps of Rho-dependent termination. First, the RNA conformation that presents an accessible rut site promotes pausing of RNA polymerase (RNAP) at a single Rho-dependent termination site over 100 nt downstream. Second, an additional RNA stem-loop promotes Rho activity and controls the location at which Rho-dependent termination occurs, despite having no effect on initial Rho binding to the corA leader. Thus, the multi-step nature of Rho-dependent termination may facilitate regulation of a given coding region by multiple cytoplasmic signals.
[Mh] Termos MeSH primário: Regulação Bacteriana da Expressão Gênica
Conformação de Ácido Nucleico
RNA Bacteriano/química
RNA Bacteriano/genética
RNA Mensageiro/química
RNA Mensageiro/genética
Fator Rho/metabolismo
Regiões Terminadoras Genéticas
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Sequência de Bases
Sítios de Ligação
Proteínas de Transporte de Cátions/metabolismo
RNA Polimerases Dirigidas por DNA/metabolismo
Ligação Proteica
RNA Bacteriano/metabolismo
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cation Transport Proteins); 0 (CorA protein, Salmonella); 0 (RNA, Bacterial); 0 (RNA, Messenger); 0 (Rho Factor); EC 2.7.7.6 (DNA-Directed RNA Polymerases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170615
[Lr] Data última revisão:
170615
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170127
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw889


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[PMID]:28082594
[Au] Autor:Yuan AH; Hochschild A
[Ad] Endereço:Department of Microbiology and Immunobiology, Harvard Medical School, 4 Blackfan Circle, Boston, MA 02115, USA.
[Ti] Título:A bacterial global regulator forms a prion.
[So] Source:Science;355(6321):198-201, 2017 01 13.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prions are self-propagating protein aggregates that act as protein-based elements of inheritance in fungi. Although prevalent in eukaryotes, prions have not been identified in bacteria. Here we found that a bacterial protein, transcription terminator Rho of Clostridium botulinum (Cb-Rho), could form a prion. We identified a candidate prion-forming domain (cPrD) in Cb-Rho and showed that it conferred amyloidogenicity on Cb-Rho and could functionally replace the PrD of a yeast prion-forming protein. Furthermore, its cPrD enabled Cb-Rho to access alternative conformations in Escherichia coli-a soluble form that terminated transcription efficiently and an aggregated, self-propagating prion form that was functionally compromised. The prion form caused genome-wide changes in the transcriptome. Thus, Cb-Rho functions as a protein-based element of inheritance in bacteria, suggesting that the emergence of prions predates the evolutionary split between eukaryotes and bacteria.
[Mh] Termos MeSH primário: Amiloide/metabolismo
Proteínas de Bactérias/metabolismo
Clostridium botulinum/metabolismo
Príons/metabolismo
Fator Rho/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Amiloide/química
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Escherichia coli/metabolismo
Evolução Molecular
Domínios Proteicos
Fator Rho/química
Fator Rho/genética
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Amyloid); 0 (Bacterial Proteins); 0 (Prions); 0 (Rho Factor); 0 (Saccharomyces cerevisiae Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170114
[St] Status:MEDLINE
[do] DOI:10.1126/science.aai7776


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[PMID]:27899597
[Au] Autor:Drögemüller J; Schneider C; Schweimer K; Strauß M; Wöhrl BM; Rösch P; Knauer SH
[Ad] Endereço:Lehrstuhl Biopolymere und Forschungszentrum für Bio-Makromoleküle, Universität Bayreuth, Universitätsstraße 30, 95447 Bayreuth, Germany.
[Ti] Título:Thermotoga maritima NusG: domain interaction mediates autoinhibition and thermostability.
[So] Source:Nucleic Acids Res;45(1):446-460, 2017 Jan 09.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:NusG, the only universally conserved transcription factor, comprises an N- and a C-terminal domain (NTD, CTD) that are flexibly connected and move independently in Escherichia coli and other organisms. In NusG from the hyperthermophilic bacterium Thermotoga maritima (tmNusG), however, NTD and CTD interact tightly. This closed state stabilizes the CTD, but masks the binding sites for the interaction partners Rho, NusE and RNA polymerase (RNAP), suggesting that tmNusG is autoinhibited. Furthermore, tmNusG and some other bacterial NusGs have an additional domain, DII, of unknown function. Here we demonstrate that tmNusG is indeed autoinhibited and that binding to RNAP may stabilize the open conformation. We identified two interdomain salt bridges as well as Phe336 as major determinants of the domain interaction. By successive weakening of this interaction we show that after domain dissociation tmNusG-CTD can bind to Rho and NusE, similar to the Escherichia coli NusG-CTD, indicating that these interactions are conserved in bacteria. Furthermore, we show that tmNusG-DII interacts with RNAP as well as nucleic acids with a clear preference for double stranded DNA. We suggest that tmNusG-DII supports tmNusG recruitment to the transcription elongation complex and stabilizes the tmNusG:RNAP complex, a necessary adaptation to high temperatures.
[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
Fator Rho/química
Thermotoga maritima/genética
Fatores de Transcrição/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Sequência Conservada
DNA/química
DNA/genética
DNA/metabolismo
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
Temperatura Alta
Fatores de Alongamento de Peptídeos/genética
Fatores de Alongamento de Peptídeos/metabolismo
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estabilidade Proteica
Estrutura Secundária de Proteína
Fator Rho/genética
Fator Rho/metabolismo
Proteínas Ribossômicas/química
Proteínas Ribossômicas/genética
Proteínas Ribossômicas/metabolismo
Relação Estrutura-Atividade
Thermotoga maritima/metabolismo
Fatores de Transcrição/genética
Fatores de Transcrição/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 (Rho Factor); 0 (Ribosomal Proteins); 0 (Transcription Factors); 0 (ribosomal protein S10); 9007-49-2 (DNA); EC 2.7.7.6 (DNA-Directed RNA Polymerases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161201
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw1111


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[PMID]:27605667
[Au] Autor:Valabhoju V; Agrawal S; Sen R
[Ad] Endereço:From the Laboratory of Transcription, Center for DNA Fingerprinting and Diagnostics, Tuljaguda Complex, 4-1-714 Mozamjahi Road, Nampally, Hyderabad 500 001, India and.
[Ti] Título:Molecular Basis of NusG-mediated Regulation of Rho-dependent Transcription Termination in Bacteria.
[So] Source:J Biol Chem;291(43):22386-22403, 2016 Oct 21.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The bacterial transcription elongation factor NusG stimulates the Rho-dependent transcription termination through a direct interaction with Rho. The mechanistic basis of NusG dependence of the Rho function is not known. Here, we describe Rho* mutants I168V, R221C/A, and P235H that do not require NusG for their termination function. These Rho* mutants have acquired new properties, which otherwise would have been imparted by NusG. A detailed analyses revealed that they have more stable interactions at the secondary RNA binding sites of Rho, which reduced the lag in initiating its ATPase as well as the translocase activities. These more stable interactions arose from the significant spatial re-orientations of the P, Q, and R structural loops of the Rho central channel. We propose that NusG imparts similar conformational changes in the central channel of Rho, yielding faster isomerization of the open to the closed hexameric states of the latter during its RNA-loading step. This acceleration stabilizes the Rho-RNA interactions at many terminators having suboptimal rut sites, thus making Rho-NusG interactions so essential in vivo Finally, identification of the NusG binding sites on the Rho hexamer led us to conclude that the former exerts its effect allosterically.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/metabolismo
Conformação de Ácido Nucleico
Fatores de Alongamento de Peptídeos/metabolismo
RNA Bacteriano/metabolismo
Fator Rho/metabolismo
Fatores de Transcrição/metabolismo
Terminação da Transcrição Genética/fisiologia
[Mh] Termos MeSH secundário: Regulação Alostérica/fisiologia
Substituição de Aminoácidos
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas de Escherichia coli/genética
Mutação de Sentido Incorreto
Fatores de Alongamento de Peptídeos/genética
RNA Bacteriano/genética
Fator Rho/genética
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (NusG protein, E coli); 0 (Peptide Elongation Factors); 0 (RNA, Bacterial); 0 (Rho Factor); 0 (Transcription Factors)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171021
[Lr] Data última revisão:
171021
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160909
[St] Status:MEDLINE


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[PMID]:27362730
[Au] Autor:Nguyen CH; Stadler S; Brenner S; Huttary N; Krieger S; Jäger W; Dolznig H; Krupitza G
[Ad] Endereço:Department for Clinical Pharmacy and Diagnostics, Faculty of Life Sciences, University of Vienna, Althanstrasse 14, A-1090 Vienna, Austria.
[Ti] Título:Cancer cell-derived 12(S)-HETE signals via 12-HETE receptor, RHO, ROCK and MLC2 to induce lymph endothelial barrier breaching.
[So] Source:Br J Cancer;115(3):364-70, 2016 Jul 26.
[Is] ISSN:1532-1827
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The arachidonic acid metabolite 12(S)-HETE is suspected to enhance metastatic spread by inducing cancer cell- and lymph endothelial cell (LEC) motility. However, the molecular mechanisms leading to 12(S)-HETE-triggered cell migration are still elusive. METHODS: To delineate the signalling pathways involved in 12(S)-HETE-mediated migration, inhibitors against RHO and ROCK, and specific siRNAs downregulating 12(S)-HETE receptor (12-HETER) and myosin light chain 2 (MLC2) were used. The breaching of the endothelial barrier was investigated by an assay measuring tumour spheroid-triggered 'circular chemorepellent-induced defects' (CCIDs), and respective signal transduction was elucidated by western blotting. RESULTS: We provide evidence that 12(S)-HETE phosphorylated (and activated) MLC2, which regulates actin/myosin-based contraction. MLC2 activation was found to be essential for LEC retraction and CCID formation. Furthermore, we show that 12(S)-HETE activated a 12-HETER-RHO-ROCK-MYPT signalling cascade to induce MLC2 function. CONCLUSIONS: Signalling via this pathway is described for this metabolite for the first time. This may provide potential targets for the intervention of metastatic colonisation.
[Mh] Termos MeSH primário: Ácido 12-Hidroxi-5,8,10,14-Eicosatetraenoico/metabolismo
Endotélio Linfático/metabolismo
Cadeias Leves de Miosina/metabolismo
Receptores Eicosanoides/metabolismo
Fator Rho/metabolismo
Transdução de Sinais
Quinases Associadas a rho/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Seres Humanos
Permeabilidade
Fosforilação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (12-hydroxyeicosatetraenoic acid receptor); 0 (Myosin Light Chains); 0 (Receptors, Eicosanoid); 0 (Rho Factor); 59985-28-3 (12-Hydroxy-5,8,10,14-eicosatetraenoic Acid); EC 2.7.11.1 (rho-Associated Kinases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160701
[St] Status:MEDLINE
[do] DOI:10.1038/bjc.2016.201


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[PMID]:27325240
[Au] Autor:Kriner MA; Sevostyanova A; Groisman EA
[Ad] Endereço:Department of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT 06536, USA; Microbial Sciences Institute, Yale University, West Haven, CT 06516, USA.
[Ti] Título:Learning from the Leaders: Gene Regulation by the Transcription Termination Factor Rho.
[So] Source:Trends Biochem Sci;41(8):690-699, 2016 Aug.
[Is] ISSN:0968-0004
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The RNA helicase Rho triggers 20-30% of transcription termination events in bacteria. While Rho is associated with most transcription elongation complexes, it only promotes termination of a subset. Recent studies of individual Rho-dependent terminators located within the 5' leader regions of bacterial mRNAs have identified novel mechanisms that govern Rho target specificity and have revealed unanticipated physiological functions for Rho. In particular, the multistep nature of Rho-dependent termination enables regulatory input from determinants beyond the sequence of the Rho loading site, and allows a given Rho-dependent terminator to respond to multiple signals. Further, the unique position of Rho as a sensor of cellular translation has been exploited to regulate the transcription of genes required for protein synthesis, including those specifying Mg(2+) transporters.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica
Fator Rho/metabolismo
Terminação da Transcrição Genética
[Mh] Termos MeSH secundário: Bactérias/genética
Bactérias/metabolismo
RNA Bacteriano/genética
RNA Bacteriano/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (RNA, Bacterial); 0 (Rho Factor)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160622
[St] Status:MEDLINE


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[PMID]:27124216
[Au] Autor:Mosrin-Huaman C; Hervouet-Coste N; Rahmouni AR
[Ad] Endereço:a Centre de Biophysique Moléculaire , Rue Charles Sadron , Orléans , France.
[Ti] Título:Co-transcriptional degradation by the 5'-3' exonuclease Rat1p mediates quality control of HXK1 mRNP biogenesis in S. cerevisiae.
[So] Source:RNA Biol;13(6):582-92, 2016 Jun 02.
[Is] ISSN:1555-8584
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The co-transcriptional biogenesis of export-competent messenger ribonucleoprotein particles (mRNPs) in yeast is under the surveillance of quality control (QC) steps. Aberrant mRNPs resulting from inappropriate or inefficient processing and packaging reactions are detected by the QC system and retained in the nucleus with ensuing elimination of their mRNA component by a mechanism that requires the catalytic activity of Rrp6p, a 3'-5' exonuclease associated with the RNA exosome. In previous studies, we implemented a new experimental approach in which the production of aberrant mRNPs is massively increased upon perturbation of mRNP biogenesis by the RNA-dependent helicase/translocase activity of the bacterial Rho factor expressed in S. cerevisiae. The analyses of a subset of transcripts such as PMA1 led us to substantiate the essential role of Rrp6p in the nuclear mRNP QC and to reveal a functional coordination of the process by Nrd1p. Here, we extended those results by showing that, in contrast to PMA1, Rho-induced aberrant HXK1 mRNPs are targeted for destruction by an Nrd1p- and Rrp6p-independent alternative QC pathway that relies on the 5'-3' exonuclease activity of Rat1p. We show that the degradation of aberrant HXK1 mRNPs by Rat1p occurs co-transcriptionally following decapping by Dcp2p and leads to premature transcription termination. We discuss the possibility that this alternative QC pathway might be linked to the well-known specific features of the HXK1 gene transcription such as its localization at the nuclear periphery and gene loop formation.
[Mh] Termos MeSH primário: Exorribonucleases/metabolismo
Hexoquinase/genética
Fator Rho/metabolismo
Ribonucleoproteína Nuclear Pequena U4-U6/metabolismo
Ribonucleoproteína Nuclear Pequena U5/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Núcleo Celular/genética
Núcleo Celular/metabolismo
Endorribonucleases/genética
ATPases Translocadoras de Prótons/genética
Controle de Qualidade
RNA Fúngico/genética
RNA Mensageiro/genética
Proteínas de Saccharomyces cerevisiae/genética
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (PRP6 protein, S cerevisiae); 0 (RNA, Fungal); 0 (RNA, Messenger); 0 (Rho Factor); 0 (Ribonucleoprotein, U4-U6 Small Nuclear); 0 (Ribonucleoprotein, U5 Small Nuclear); 0 (Saccharomyces cerevisiae Proteins); 147883-15-6 (RAT1 protein, S cerevisiae); EC 2.7.1.1 (Hexokinase); EC 3.1.- (DCP2 protein, S cerevisiae); EC 3.1.- (Endoribonucleases); EC 3.1.- (Exoribonucleases); EC 3.6.1.- (PMA1 protein, S cerevisiae); EC 3.6.3.14 (Proton-Translocating ATPases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171011
[Lr] Data última revisão:
171011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160429
[St] Status:MEDLINE
[do] DOI:10.1080/15476286.2016.1181255



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