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[PMID]:28654657
[Au] Autor:Termini JM; Silver ZA; Connor B; Antonopoulos A; Haslam SM; Dell A; Desrosiers RC
[Ad] Endereço:Department of Pathology, University of Miami Miller School of Medicine, Miami, Florida, United States of America.
[Ti] Título:HEK293T cell lines defective for O-linked glycosylation.
[So] Source:PLoS One;12(6):e0179949, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Here we describe derivatives of the HEK293T cell line that are defective in their ability to generate mucin-type O-linked glycosylation. Using CRISPR/Cas9 and a single-cell GFP-sorting procedure, the UDP-galactose-4-epimerase (GALE), galactokinase 1 (GALK1), and galactokinase 2 (GALK2) genes were knocked out individually and in combinations with greater than 90% of recovered clones having the desired mutations. Although HEK293T cells are tetraploid, we found this approach to be an efficient method to target and disrupt all 4 copies of the target gene. Deficient glycosylation in the GALE knockout cell line could be rescued by the addition of galactose and N-acetylgalactosamine (GalNAc) to the cell culture media. However, when key enzymes of the galactose/GalNAc salvage pathways were disrupted in tandem (GALE+GALK1 or GALE+GALK2), O-glycosylation was eliminated and could not be rescued by the addition of either galactose plus GalNAc or UDP-galactose plus UDP-GalNAc. GALK1 and GALK2 are key enzymes of the galactose/GalNAc salvage pathways. Mass spectrometry was performed on whole cell lysate of the knockout cell lines to verify the glycosylation phenotype. As expected, the GALE knockout was almost completely devoid of all O-glycosylation, with minimal glycosylation as a result of functional salvage pathways. However, the GALE+GALK1 and GALE+GALK2 knockout lines were devoid of all O-glycans. Mass spectrometry analysis revealed that the disruption of GALE, GALK1, and GALE+GALK2 had little effect on the N-glycome. But when GALE was knocked out in tandem with GALK1, N-glycans were exclusively of the high mannose type. Due to the well-characterized nature of these five knockout cell lines, they will likely prove useful for a wide variety of applications.
[Mh] Termos MeSH primário: Galactoquinase/genética
UDPglucose 4-Epimerase/genética
[Mh] Termos MeSH secundário: Galactoquinase/metabolismo
Técnicas de Inativação de Genes
Glucanos/metabolismo
Glicosilação
Células HEK293
Seres Humanos
Espectrometria de Massas
UDPglucose 4-Epimerase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucans); EC 2.7.1.6 (GALK1 protein, human); EC 2.7.1.6 (GALK2 protein, human); EC 2.7.1.6 (Galactokinase); EC 5.1.3.2 (UDPglucose 4-Epimerase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179949


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[PMID]:28254434
[Au] Autor:Zacharioudakis I; Tzamarias D
[Ad] Endereço:Biology Department, University of Crete, Heraklion, Crete, Greece.
[Ti] Título:Bimodal expression of yeast GAL genes is controlled by a long non-coding RNA and a bifunctional galactokinase.
[So] Source:Biochem Biophys Res Commun;486(1):63-69, 2017 Apr 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bimodality in gene expression can generate phenotypic heterogeneity facilitating fitness and growth of isogenic cell populations in suboptimal environments. We investigated the mechanism by which, in conditions of limiting galactose, yeast cell populations activate GAL genes in a bimodal fashion with a cell fraction expressing GAL genes (ON), while the rest subpopulation is kept at the non-expressing (OFF) state. We show that a long non-coding RNA (GAL10-ncRNA) crossing the bidirectional GAL1-10 promoter, decreases the rate by which single cells commit transition to the ON state without affecting the rate of GAL transcription per se in ON cells. This is accomplished by repressing stochastic expression of the bifunctional Gal1p galactokinase, which besides its enzymatic activity acts as an essential inducer of the system under those conditions. We show that once single cells switch to the ON state, the GAL10-ncRNA effect is overridden by accumulating Gal1p levels sufficient to feedback positively on Gal4p, and not by the active transcription of GAL10 that occurs in opposite direction relative to that of GAL10-ncRNA. Conversely, GAL10-ncRNA does not influence transition of ON cells, where Gal4p is active, back to the OFF state. Our model suggests that the functional interplay between GAL10-ncRNA transcription, stochastic Gal1p expression and Gal1p positive feedback on Gal4p constitutes a novel molecular switch mechanism dictating the commitment of individual cells for either metabolic state.
[Mh] Termos MeSH primário: Galactoquinase/genética
Regulação Enzimológica da Expressão Gênica
Regulação Fúngica da Expressão Gênica
RNA Longo não Codificante/genética
Proteínas de Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Retroalimentação Fisiológica
Galactoquinase/metabolismo
Galactose/metabolismo
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Microscopia de Fluorescência
Modelos Genéticos
Mutação
Regiões Promotoras Genéticas/genética
RNA Fúngico/genética
Saccharomyces cerevisiae/citologia
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Análise de Célula Única/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Fungal); 0 (RNA, Long Noncoding); 0 (Saccharomyces cerevisiae Proteins); 147336-22-9 (Green Fluorescent Proteins); EC 2.7.1.6 (Galactokinase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170619
[Lr] Data última revisão:
170619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170304
[St] Status:MEDLINE


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[PMID]:28180315
[Au] Autor:Aibara S; Gordon JM; Riesterer AS; McLaughlin SH; Stewart M
[Ad] Endereço:MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, UK
[Ti] Título:Structural basis for the dimerization of Nab2 generated by RNA binding provides insight into its contribution to both poly(A) tail length determination and transcript compaction in Saccharomyces cerevisiae.
[So] Source:Nucleic Acids Res;45(3):1529-1538, 2017 02 17.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In Saccharomyces cerevisiae generation of export-competent mRNPs terminates the nuclear phase of the gene expression pathway and facilitates transport to the cytoplasm for translation. Nab2 functions in this process to control both mRNP compaction that facilitates movement through nuclear pore complexes and the length of transcript poly(A) tails. Nab2 has a modular structure that includes seven CCCH Zn fingers that bind to A-rich RNAs and fingers 5­7 are critical for these functions. Here, we demonstrate, using both biophysical and structural methods, that binding A11G RNA induces dimerization of Zn fingers 5­7 mediated by the novel spatial arrangement of the fingers promoting each RNA chain binding two protein chains. The dimerization of Nab2 induced by RNA binding provides a basis for understanding its function in both poly(A) tail length regulation and in the compaction of mature transcripts to facilitate nuclear export.
[Mh] Termos MeSH primário: Proteínas de Transporte Nucleocitoplasmático/química
Proteínas de Transporte Nucleocitoplasmático/metabolismo
RNA Fúngico/metabolismo
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/metabolismo
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Substituição de Aminoácidos
Sequência de Bases
Fenômenos Biofísicos
Cristalografia por Raios X
Galactoquinase/genética
Genes Fúngicos
Modelos Moleculares
Mutagênese Sítio-Dirigida
Proteínas de Transporte Nucleocitoplasmático/genética
Poliadenilação
Domínios Proteicos
Multimerização Proteica
RNA Fúngico/química
RNA Fúngico/genética
RNA Mensageiro/química
RNA Mensageiro/genética
Proteínas de Ligação a RNA/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Dedos de Zinco
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NAB2 protein, S cerevisiae); 0 (Nucleocytoplasmic Transport Proteins); 0 (RNA, Fungal); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (Recombinant Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 2.7.1.6 (GAL1 protein, S cerevisiae); EC 2.7.1.6 (Galactokinase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170210
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw1224


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[PMID]:28137775
[Au] Autor:Stockwell SR; Rifkin SA
[Ad] Endereço:Section of Ecology, Behavior, and Evolution, Division of Biological Sciences, University of California, San Diego La Jolla, CA, USA.
[Ti] Título:A living vector field reveals constraints on galactose network induction in yeast.
[So] Source:Mol Syst Biol;13(1):908, 2017 Jan 30.
[Is] ISSN:1744-4292
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:When a cell encounters a new environment, its transcriptional response can be constrained by its history. For example, yeast cells in galactose induce GAL genes with a speed and unanimity that depends on previous nutrient conditions. Cellular memory of long-term glucose exposure delays GAL induction and makes it highly variable with in a cell population, while other nutrient histories lead to rapid, uniform responses. To investigate how cell-level gene expression dynamics produce population-level phenotypes, we built living vector fields from thousands of single-cell time courses of the proteins Gal3p and Gal1p as cells switched to galactose from various nutrient histories. We show that, after sustained glucose exposure, the lack of these GAL transducers leads to induction delays that are long but also variable; that cellular resources constrain induction; and that bimodally distributed expression levels arise from lineage selection-a subpopulation of cells induces more quickly and outcompetes the rest. Our results illuminate cellular memory in this important model system and illustrate how resources and randomness interact to shape the response of a population to a new environment.
[Mh] Termos MeSH primário: Galactoquinase/genética
Galactose/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/crescimento & desenvolvimento
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Regulação Fúngica da Expressão Gênica
Redes Reguladoras de Genes
Óperon
Fenótipo
Saccharomyces cerevisiae/genética
Análise de Célula Única
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gal3 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factors); EC 2.7.1.6 (GAL1 protein, S cerevisiae); EC 2.7.1.6 (Galactokinase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE
[do] DOI:10.15252/msb.20167323


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[PMID]:28057307
[Au] Autor:Daenzer JM; Fridovich-Keil JL
[Ad] Endereço:Emory University School of Medicine, Atlanta, GA, United States.
[Ti] Título:Drosophila melanogaster Models of Galactosemia.
[So] Source:Curr Top Dev Biol;121:377-395, 2017.
[Is] ISSN:1557-8933
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The galactosemias are a family of autosomal recessive genetic disorders resulting from impaired function of the Leloir pathway of galactose metabolism. Type I, or classic galactosemia, results from profound deficiency of galactose-1-phosphate uridylyltransferase, the second enzyme in the Leloir pathway. Type II galactosemia results from profound deficiency of galactokinase, the first enzyme in the Leloir pathway. Type III galactosemia results from partial deficiency of UDP galactose 4'-epimerase, the third enzyme in the Leloir pathway. Although at least classic galactosemia has been recognized clinically for more than 100 years, and detectable by newborn screening for more than 50 years, all three galactosemias remain poorly understood. Early detection and dietary restriction of galactose prevent neonatal lethality, but many affected infants grow to experience a broad range of developmental and other disabilities. To date, there is no intervention known that prevents or reverses these long-term complications. Drosophila melanogaster provides a genetically and biochemically facile model for these conditions, enabling studies that address mechanism and open the door for novel approaches to intervention.
[Mh] Termos MeSH primário: Modelos Animais de Doenças
Drosophila melanogaster/fisiologia
Galactosemias/patologia
UDPglucose 4-Epimerase/metabolismo
[Mh] Termos MeSH secundário: Animais
Galactoquinase/metabolismo
Galactose/metabolismo
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 2.7.1.6 (Galactokinase); EC 5.1.3.2 (UDPglucose 4-Epimerase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171115
[Lr] Data última revisão:
171115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170107
[St] Status:MEDLINE


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[PMID]:27789348
[Au] Autor:McAuley M; Huang M; Timson DJ
[Ad] Endereço:School of Biological Sciences, Queen's University Belfast, Medical Biology Building, 97 Lisburn Road, Belfast BT9 7BL, UK.
[Ti] Título:Insight into the mechanism of galactokinase: Role of a critical glutamate residue and helix/coil transitions.
[So] Source:Biochim Biophys Acta;1865(3):321-328, 2017 03.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Galactokinase, the enzyme which catalyses the first committed step in the Leloir pathway, has attracted interest due to its potential as a biocatalyst and as a possible drug target in the treatment of type I galactosemia. The mechanism of the enzyme is not fully elucidated. Molecular dynamics (MD) simulations of galactokinase with the active site residues Arg-37 and Asp-186 altered predicted that two regions (residues 174-179 and 231-240) had different dynamics as a consequence. Interestingly, the same two regions were also affected by alterations in Arg-105, Glu-174 and Arg-228. These three residues were identified as important in catalysis in previous computational studies on human galactokinase. Alteration of Arg-105 to methionine resulted in a modest reduction in activity with little change in stability. When Arg-228 was changed to methionine, the enzyme's interaction with both ATP and galactose was affected. This variant was significantly less stable than the wild-type protein. Changing Glu-174 to glutamine (but not to aspartate) resulted in no detectable activity and a less stable enzyme. Overall, these combined in silico and in vitro studies demonstrate the importance of a negative charge at position 174 and highlight the critical role of the dynamics in to key regions of the protein. We postulate that these regions may be critical for mediating the enzyme's structure and function.
[Mh] Termos MeSH primário: Galactoquinase/metabolismo
Ácido Glutâmico/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Ácido Aspártico/metabolismo
Catálise
Domínio Catalítico/fisiologia
Galactose/metabolismo
Galactosemias/metabolismo
Seres Humanos
Metionina/metabolismo
Simulação de Dinâmica Molecular
Conformação Proteica
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
30KYC7MIAI (Aspartic Acid); 3KX376GY7L (Glutamic Acid); 8L70Q75FXE (Adenosine Triphosphate); AE28F7PNPL (Methionine); EC 2.7.1.6 (Galactokinase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161030
[St] Status:MEDLINE


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[PMID]:27714848
[Au] Autor:Meurer M; Chevyreva V; Cerulus B; Knop M
[Ad] Endereço:Zentrum für Molekulare Biologie der Universität Heidelberg, University of Heidelberg, Im Neuenheimer Feld 282, 69120, Heidelberg, Germany.
[Ti] Título:The regulatable MAL32 promoter in Saccharomyces cerevisiae: characteristics and tools to facilitate its use.
[So] Source:Yeast;34(1):39-49, 2017 Jan.
[Is] ISSN:1097-0061
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Here we describe a set of tools to facilitate the use of maltose and the MAL32 promoter for regulated gene expression in yeast, alone or in combination with the GAL1 promoter. Using fluorescent protein reporters we find that under non-inducing conditions the MAL32 promoter exhibits a low basal level of expression, similar to the GAL1 promoter, and that both promoters can be induced independently of each other using the respective sugars, maltose and galactose. While their repression upon glucose addition is immediate and complete, we found that the MAL32 and GAL1 promoters each exhibit distinct induction kinetics. A set of plasmids is available to facilitate the application of the MAL32 promoter for chromosomal modifications using PCR targetting and for plasmid based gene expression. Copyright © 2016 John Wiley & Sons, Ltd.
[Mh] Termos MeSH primário: Regiões Promotoras Genéticas/genética
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Citometria de Fluxo
Galactoquinase/genética
Galactoquinase/fisiologia
Regulação Fúngica da Expressão Gênica/genética
Regulação Fúngica da Expressão Gênica/fisiologia
Glucose/metabolismo
Maltose/metabolismo
Regiões Promotoras Genéticas/fisiologia
Saccharomyces cerevisiae/fisiologia
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Saccharomyces cerevisiae Proteins); 69-79-4 (Maltose); EC 2.7.1.6 (GAL1 protein, S cerevisiae); EC 2.7.1.6 (Galactokinase); IY9XDZ35W2 (Glucose)
[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:161008
[St] Status:MEDLINE
[do] DOI:10.1002/yea.3214


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[PMID]:27919945
[Au] Autor:Tang M; Etokidem E; Lai K
[Ad] Endereço:Division of Medical Genetics, Department of Pediatrics, University of Utah School of Medicine, Salt Lake City, UT, U.S.A. manshu.tang@hsc.utah.edu kent.lai@hsc.utah.edu.
[Ti] Título:The Leloir Pathway of Galactose Metabolism - A Novel Therapeutic Target for Hepatocellular Carcinoma.
[So] Source:Anticancer Res;36(12):6265-6271, 2016 12.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Hepatocellular carcinoma (HCC) is one of the most lethal types of cancer worldwide, with poor prognosis and limited treatments. In order to identify novel therapeutic targets that will lead to development of effective therapies with manageable side effects, we tested the hypothesis that knocking-down galactokinase (GALK1) or galactose-1 phosphate uridylyltransferase (GALT) gene expression would control the growth of cultured hepatoma cells. Our results showed small interfering RNA (siRNA) against GALK1 or GALT inhibited the growth of HepG2 cells in culture. Western blot analysis revealed simultaneous down-regulation of multiple players of the phosphatidylinositol 3-kinase (PI3K)/protein kinase B (AKT) growth signaling pathway, as well as heat-shock protein 90 (HSP90) and poly ADP ribose polymerase (PARP). Reverse transcription-polymerase chain reaction (RT-PCR) data, however, showed no significant mRNA reduction of the encoded genes. Our study thus not only supports GALK1 and GALT as being possible novel targets for treating HCC, but also uncovers new post-transcriptional regulatory mechanisms that link the galactose metabolic pathway to protein expression of the PI3K/AKT pathway in hepatoma.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/metabolismo
Galactose/metabolismo
Neoplasias Hepáticas/terapia
[Mh] Termos MeSH secundário: Carcinoma Hepatocelular/terapia
Galactoquinase/genética
Galactoquinase/metabolismo
Células Hep G2
Seres Humanos
Neoplasias Hepáticas/metabolismo
RNA Interferente Pequeno
UTP-Hexose-1-Fosfato Uridililtransferase/genética
UTP-Hexose-1-Fosfato Uridililtransferase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Small Interfering); EC 2.7.1.6 (GALK1 protein, human); EC 2.7.1.6 (Galactokinase); EC 2.7.7.10 (UTP-Hexose-1-Phosphate Uridylyltransferase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170830
[Lr] Data última revisão:
170830
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161207
[St] Status:MEDLINE


  9 / 677 MEDLINE  
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[PMID]:27700226
[Au] Autor:Beck ZT; Xing Z; Tran EJ
[Ad] Endereço:a Department of Biochemistry , Purdue University , West Lafayette , IN , USA.
[Ti] Título:LncRNAs: Bridging environmental sensing and gene expression.
[So] Source:RNA Biol;13(12):1189-1196, 2016 Dec.
[Is] ISSN:1555-8584
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The survival of all organisms is dependent on complex, coordinated responses to environmental cues. Non-coding RNAs have been identified as major players in regulation of gene expression, with recent evidence supporting roles for long non-coding (lnc)RNAs in both transcriptional and post-transcriptional control. Evidence from our laboratory shows that lncRNAs have the ability to form hybridized structures called R-loops with specific DNA target sequences in S. cerevisiae, thereby modulating gene expression. In this Point of View, we provide an overview of the nature of lncRNA-mediated control of gene expression in the context of our studies using the GAL gene cluster as a model for controlling the timing of transcription.
[Mh] Termos MeSH primário: DNA Fúngico/metabolismo
RNA Longo não Codificante/genética
Saccharomyces cerevisiae/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Proteínas Fúngicas/química
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
Galactoquinase/química
Galactoquinase/genética
Galactoquinase/metabolismo
Regulação Fúngica da Expressão Gênica
Conformação de Ácido Nucleico
RNA Fúngico/química
RNA Fúngico/genética
RNA Longo não Codificante/química
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Transativadores/química
Transativadores/genética
Transativadores/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Fungal); 0 (Fungal Proteins); 0 (GAL10 protein, S cerevisiae); 0 (RNA, Fungal); 0 (RNA, Long Noncoding); 0 (Saccharomyces cerevisiae Proteins); 0 (Trans-Activators); EC 2.7.1.6 (GAL1 protein, S cerevisiae); EC 2.7.1.6 (Galactokinase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161005
[St] Status:MEDLINE


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[PMID]:27630054
[Au] Autor:Jónás Á; Fekete E; Németh Z; Flipphi M; Karaffa L
[Ad] Endereço:Department of Biochemical Engineering, Faculty of Science and Technology, University of Debrecen , H-4032, P.O. Box 64, Debrecen , Hungary.
[Ti] Título:D-galactose catabolism in Penicillium chrysogenum: Expression analysis of the structural genes of the Leloir pathway.
[So] Source:Acta Biol Hung;67(3):318-32, 2016 Sep.
[Is] ISSN:0236-5383
[Cp] País de publicação:Hungary
[La] Idioma:eng
[Ab] Resumo:In this study, we analyzed the expression of the structural genes encoding the five enzymes comprising the Leloir pathway of D-galactose catabolism in the industrial cell factory Penicillium chrysogenum on various carbon sources. The genome of P. chrysogenum contains a putative galactokinase gene at the annotated locus Pc13g10140, the product of which shows strong structural similarity to yeast galactokinase that was expressed on lactose and D-galactose only. The expression profile of the galactose-1-phosphate uridylyl transferase gene at annotated locus Pc15g00140 was essentially similar to that of galactokinase. This is in contrast to the results from other fungi such as Aspergillus nidulans, Trichoderma reesei and A. niger, where the ortholog galactokinase and galactose-1-phosphate uridylyl transferase genes were constitutively expressed. As for the UDP-galactose-4-epimerase encoding gene, five candidates were identified. We could not detect Pc16g12790, Pc21g12170 and Pc20g06140 expression on any of the carbon sources tested, while for the other two loci (Pc21g10370 and Pc18g01080) transcripts were clearly observed under all tested conditions. Like the 4-epimerase specified at locus Pc21g10370, the other two structural Leloir pathway genes - UDP-glucose pyrophosphorylase (Pc21g12790) and phosphoglucomutase (Pc18g01390) - were expressed constitutively at high levels as can be expected from their indispensable function in fungal cell wall formation.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Enzimas/metabolismo
Galactose/metabolismo
Penicillium chrysogenum/enzimologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Enzimas/genética
Fermentação
Galactoquinase/genética
Galactoquinase/metabolismo
Regulação Bacteriana da Expressão Gênica
Regulação Enzimológica da Expressão Gênica
Nucleotidiltransferases/genética
Nucleotidiltransferases/metabolismo
Penicillium chrysogenum/genética
Penicillium chrysogenum/crescimento & desenvolvimento
Fosfoglucomutase/genética
Fosfoglucomutase/metabolismo
Especificidade por Substrato
Fatores de Tempo
UDPglucose 4-Epimerase/genética
UDPglucose 4-Epimerase/metabolismo
UTP-Glucose-1-Fosfato Uridililtransferase/genética
UTP-Glucose-1-Fosfato Uridililtransferase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Enzymes); EC 2.7.1.6 (Galactokinase); EC 2.7.7.- (Nucleotidyltransferases); EC 2.7.7.9 (UTP-Glucose-1-Phosphate Uridylyltransferase); EC 5.1.3.2 (UDPglucose 4-Epimerase); EC 5.4.2.2 (Phosphoglucomutase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160916
[St] Status:MEDLINE
[do] DOI:10.1556/018.67.2016.3.9



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