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Setsuko Komatsu - One of the best experts on this subject based on the ideXlab platform.
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Identification of rice root proteins regulated by gibberellin using proteome analysis
Plant Cell and Environment, 2005Co-Authors: H. Konishi, Hidemi Kitano, Setsuko KomatsuAbstract:Gibberellin (GA) promoted rice (Oryza sativa L.) root elongation in a concentration-dependent manner with roots grown in 0.1 micromolar GA3 being 13.8% longer than controls. On the other hand, the roots of Tan-ginbozu, a semi-dwarf cultivar were 69.8% shorter in comparison with Nipponbare, a normal cultivar. Treatments with 10 micromolar uniconazole-P and 10 micromolar abscisic acid (ABA) caused decreases in root length in Tan-ginbozu by 44.6 and 79.2%, respectively. To investigate how GA influences rice root growth, proteome analysis techniques were applied. Extracted proteins were separated by two-dimensional polyacrylamide gel electrophoresis and analysed using an automated protein sequencer and mass spectrometer. Sixteen proteins show differences in accumulation levels as a result of treatment with GA3, uniconazole-P and ABA treatment and/or the difference between the semi-dwarf cultivar, Tan-ginbozu, and normal cultivars. Among these proteins, Fructose-Bisphosphate aldolase (EC 4.1.2.13) increased in roots treated with GA3, occurred in low levels in Tan-ginbozu roots, and decreased in roots treated with uniconazole-P or ABA. Moreover, roots from seedlings grown in 100 micromolar glucose were 9.1% longer than controls. These results indicate that increases in Fructose-Bisphosphate aldolase activity stimulate the glycolytic pathway and may play an important role in the GA-induced growth of roots.
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Characterization of Fructose-Bisphosphate aldolase regulated by gibberellin in roots of rice seedling
Plant Molecular Biology, 2004Co-Authors: Hirosato Konishi, Hisakazu Yamane, Masayoshi Maeshima, Setsuko KomatsuAbstract:Fructose-Bisphosphate aldolase is a glycolytic enzyme whose activity increases in rice roots treated with gibberellin (GA). To investigate the relationship between aldolase and root growth, GA-induced root aldolase was characterized. GA_3 promoted an increase in aldolase accumulation when 0.1 μ M GA_3 was added exogenously to rice roots. Aldolase accumulated abundantly in roots, especially in the apical region. To examine the effect of aldolase function on root growth, transgenic rice plants expressing antisense aldolase were constructed. Root growth of aldolase-antisense transgenic rice was repressed compared with that of the vector control transgenic rice. Although aldolase activity increased by 25% in vector control rice roots treated with 0.1 μ M GA_3, FBPA activity increased very little by 0.1 μ M GA_3 treatment in the root of aldolase-antisense transgenic rice. Furthermore, aldolase co-immunoprecipitated with antibodies against vacuolar H^+-ATPase in rice roots. In the root of OsCDPK13-antisense transgenic rice, aldolase did not accumulate even after treatment with GA_3. These results suggest that the activation of glycolytic pathway function accelerates root growth and that GA_3-induced root aldolase may be modulated through OsCDPK13. Aldolase physically associates with vacuolar H-ATPase in roots and may regulate the vacuolar H-ATPase mediated control of cell elongation that determines root length.
Marion Dupuis - One of the best experts on this subject based on the ideXlab platform.
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the metabolic enzyme Fructose 1 6 Bisphosphate aldolase acts as a transcriptional regulator in pathogenic francisella
Nature Communications, 2017Co-Authors: Jason Ziveri, Fabiola Tros, Ida Chiara Guerrera, Cerina Chhuon, Mathilde Audry, Marion DupuisAbstract:The enzyme Fructose-Bisphosphate aldolase occupies a central position in glycolysis and gluconeogenesis pathways. Beyond its housekeeping role in metabolism, Fructose-Bisphosphate aldolase has been involved in additional functions and is considered as a potential target for drug development against pathogenic bacteria. Here, we address the role of Fructose-Bisphosphate aldolase in the bacterial pathogen Francisella novicida. We demonstrate that Fructose-Bisphosphate aldolase is important for bacterial multiplication in macrophages in the presence of gluconeogenic substrates. In addition, we unravel a direct role of this metabolic enzyme in transcription regulation of genes katG and rpoA, encoding catalase and an RNA polymerase subunit, respectively. We propose a model in which Fructose-Bisphosphate aldolase participates in the control of host redox homeostasis and the inflammatory immune response. The enzyme Fructose-Bisphosphate aldolase (FBA) plays central roles in glycolysis and gluconeogenesis. Here, Ziveri et al. show that FBA of the pathogen Francisella novicida acts, in addition, as a transcriptional regulator and is important for bacterial multiplication in macrophages.
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The metabolic enzyme Fructose-1,6-Bisphosphate aldolase acts as a transcriptional regulator in pathogenic Francisella
Nature Communications, 2017Co-Authors: Jason Ziveri, Fabiola Tros, Ida Chiara Guerrera, Cerina Chhuon, Mathilde Audry, Marion Dupuis, Monique Barel, Sarantis Korniotis, Simon Fillatreau, Lara GalesAbstract:The enzyme Fructose-Bisphosphate aldolase occupies a central position in glycolysis and gluconeogenesis pathways. Beyond its housekeeping role in metabolism, Fructose-Bisphosphate aldolase has been involved in additional functions and is considered as a potential target for drug development against pathogenic bacteria. Here, we address the role of Fructose-Bisphosphate aldolase in the bacterial pathogen Francisella novicida. We demonstrate that Fructose-Bisphosphate aldolase is important for bacterial multiplication in macrophages in the presence of gluconeogenic substrates. In addition, we unravel a direct role of this metabolic enzyme in transcription regulation of genes katG and rpoA, encoding catalase and an RNA polymerase subunit, respectively. We propose a model in which Fructose-Bisphosphate aldolase participates in the control of host redox homeostasis and the inflammatory immune response.
Jason Ziveri - One of the best experts on this subject based on the ideXlab platform.
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the metabolic enzyme Fructose 1 6 Bisphosphate aldolase acts as a transcriptional regulator in pathogenic francisella
Nature Communications, 2017Co-Authors: Jason Ziveri, Fabiola Tros, Ida Chiara Guerrera, Cerina Chhuon, Mathilde Audry, Marion DupuisAbstract:The enzyme Fructose-Bisphosphate aldolase occupies a central position in glycolysis and gluconeogenesis pathways. Beyond its housekeeping role in metabolism, Fructose-Bisphosphate aldolase has been involved in additional functions and is considered as a potential target for drug development against pathogenic bacteria. Here, we address the role of Fructose-Bisphosphate aldolase in the bacterial pathogen Francisella novicida. We demonstrate that Fructose-Bisphosphate aldolase is important for bacterial multiplication in macrophages in the presence of gluconeogenic substrates. In addition, we unravel a direct role of this metabolic enzyme in transcription regulation of genes katG and rpoA, encoding catalase and an RNA polymerase subunit, respectively. We propose a model in which Fructose-Bisphosphate aldolase participates in the control of host redox homeostasis and the inflammatory immune response. The enzyme Fructose-Bisphosphate aldolase (FBA) plays central roles in glycolysis and gluconeogenesis. Here, Ziveri et al. show that FBA of the pathogen Francisella novicida acts, in addition, as a transcriptional regulator and is important for bacterial multiplication in macrophages.
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The metabolic enzyme Fructose-1,6-Bisphosphate aldolase acts as a transcriptional regulator in pathogenic Francisella
Nature Communications, 2017Co-Authors: Jason Ziveri, Fabiola Tros, Ida Chiara Guerrera, Cerina Chhuon, Mathilde Audry, Marion Dupuis, Monique Barel, Sarantis Korniotis, Simon Fillatreau, Lara GalesAbstract:The enzyme Fructose-Bisphosphate aldolase occupies a central position in glycolysis and gluconeogenesis pathways. Beyond its housekeeping role in metabolism, Fructose-Bisphosphate aldolase has been involved in additional functions and is considered as a potential target for drug development against pathogenic bacteria. Here, we address the role of Fructose-Bisphosphate aldolase in the bacterial pathogen Francisella novicida. We demonstrate that Fructose-Bisphosphate aldolase is important for bacterial multiplication in macrophages in the presence of gluconeogenic substrates. In addition, we unravel a direct role of this metabolic enzyme in transcription regulation of genes katG and rpoA, encoding catalase and an RNA polymerase subunit, respectively. We propose a model in which Fructose-Bisphosphate aldolase participates in the control of host redox homeostasis and the inflammatory immune response.
Alan Berry - One of the best experts on this subject based on the ideXlab platform.
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a thermostable variant of Fructose Bisphosphate aldolase constructed by directed evolution also shows increased stability in organic solvents
Protein Engineering Design & Selection, 2004Co-Authors: Alan BerryAbstract:: Thermostable variants of the Class II Fructose Bisphosphate aldolase have been isolated following four rounds of directed evolution using DNA shuffling of the fda genes from Escherichia coli and Edwardsiella ictaluri. Variants from all four generations of evolution have been purified and characterized. The variants show increased thermostability with no loss of catalytic function at room temperature. The temperature at which 50% of the initial enzyme activity is lost after incubation for 10 min (T50) of the most stable variant, 4-43D6, is increased by 11-12 degrees C over the wild-type enzymes and the half-life of activity at 53 degrees C is increased approximately 190-fold. In addition, variant 4-43D6 shows increased stability to treatment with organic solvents. DNA sequencing of the evolved variants has identified the mutations which have been introduced and which lead to increased thermostability, and the role of the mutations introduced is discussed.
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the dhna gene of escherichia coli encodes a class i Fructose Bisphosphate aldolase
Biochemical Journal, 1998Co-Authors: Graeme J Thomson, Geoffrey J Howlett, Alison E Ashcroft, Alan BerryAbstract:The gene encoding the Escherichia coli Class I Fructose-1, 6-Bisphosphate aldolase (FBP aldolase) has been cloned and the protein overproduced in high amounts. This gene sequence has previously been identified as encoding an E. coli dehydrin in the GenBanktrade mark database [gene dhnA; entry code {"type":"entrez-nucleotide","attrs":{"text":"U73760","term_id":"1658027","term_text":"U73760"}}U73760; Close and Choi (1996) Submission to GenBanktrade mark]. However, the purified protein overproduced from the dhnA gene shares all its properties with those known for the E. coli Class I FBP aldolase. The protein is an 8-10-mer with a native molecular mass of approx. 340 kDa, each subunit consisting of 349 amino acids. The Class I enzyme shows low sequence identity with other known FBP aldolases, both Class I and Class II (in the order of 20%), which may be reflected by some novel properties of this FBP aldolase. The active-site peptide has been isolated and the Schiff-base-forming lysine residue (Lys236) has been identified by a combination of site-directed mutagenesis, kinetics and electrospray-ionization MS. A second lysine residue (Lys238) has been implicated in substrate binding. The cloning of this gene and the high levels of overexpression obtained will facilitate future structure-function studies.
Caihuan Ke - One of the best experts on this subject based on the ideXlab platform.
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Proteomic analysis of trochophore and veliger larvae development in the small abalone Haliotis diversicolor
BMC Genomics, 2017Co-Authors: Guilan Di, Xiulian Miao, Miaoqin Huang, Weiwei You, Yifang Zhang, Yuting Gu, Xianghui Kong, Jianxin Zhang, Caihuan KeAbstract:BackgroundHaliotis diversicolor is commercially important species. The trochophore and veliger are distinct larval stages in gastropod development. Their development involves complex morphological and physiological changes. We studied protein changes during the embryonic development of H. diversicolor using two dimensional electrophoresis (2-DE) and label-free methods, tandem mass spectrometry (MS/ MS), and Mascot for protein identification.ResultsA total of 150 2-DE gel spots were identified. Protein spots showed upregulation of 15 proteins and downregulation of 28 proteins as H. diversicolor developed from trochophore to veliger larvae. Trochophore and veliger larvae were compared using a label-free quantitative proteomic approach. A total of 526 proteins were identified from both samples, and 104 proteins were differentially expressed (> 1.5 fold). Compared with trochophore larvae, veliger larvae had 55 proteins upregulated and 49 proteins downregulated. These differentially expressed proteins were involved in shell formation, energy metabolism, cellular and stress response processes, protein synthesis and folding, cell cycle, and cell fate determination. Compared with the 5 protein (Fructose-Bisphosphate aldolase, 14–3-3ε, profilin, actin-depolymerizing factor (ADF)/cofilin) and calreticulin) expression patterns, the mRNA expression exhibited similar patterns except gene of Fructose-Bisphosphate aldolase.ConclusionOur results provide insight into novel aspects of protein function in shell formation, torsion, and nervous system development, and muscle system differentiation in H. diversicolor larvae. “Quality control” proteins were identified to be involved in abalone larval development.
