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Transcriptome analysis upon Sin3A or Sam-S knockdown or both in Drosophila cultured S2 cells

ABSTRACT: The SIN3 histone modifying complex regulates the expression of multiple methionine catabolic genes including SAM synthetase (Sam-S) as well as the level of S-adenosyl-methionine (SAM). To further investigate the relationship between methionine catabolism and epigenetic regulation by SIN3, we identified genes controlled by SIN3 and SAM-S. As a global transcriptional regulator, SIN3 impacted a wide range of genes. Independently, SAM-S affected a narrow range of genes. Additional genes, however, were influenced in dual knockdown cells. At some genes, SIN3 and SAM-S act independently, for others, redundantly and for a third set, in opposition. Together, the results obtained in the study of SIN3, a cofactor associated with histone modification, and SAM-S, a metabolic enzyme, uncover a complex relationship on regulating transcription.

ORGANISM(S): Drosophila melanogaster

PROVIDER: GSE129145 | GEO | 2019/11/26

REPOSITORIES: GEO

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Project description:Reyes-Palomares2012 - a combined model hepatic polyamine and sulfur aminoacid metabolism - version2 Mammalian polyamine metabolism consists of a bi-cycle with two required entrances, omithine and S-adenosyl methionine (SAM), and several alternative exists. The relevant regulatory roles of the short half-life enzymes ornithine decarboxylase (ODC), S-adenosyl methione decarboxylase (SAMDC) and spermindine/spermine acetyl transferase (SSAT) in polyamine metabolism are well studied, and has been modelled here. This model is described in the article: A combined model of hepatic polyamine and sulfur amino acid metabolism to analyze S-adenosyl methionine availability. Reyes-Palomares A, Montañez R, Sánchez-Jiménez F, Medina MA Amino Acids, February 2012, Volume 42, Issue 2-3, pp 597-610 Abstract: Many molecular details remain to be uncovered concerning the regulation of polyamine metabolism. A previous model of mammalian polyamine metabolism showed that S-adenosyl methionine availability could play a key role in polyamine homeostasis. To get a deeper insight in this prediction, we have built a combined model by integration of the previously published polyamine model and one-carbon and glutathione metabolism model, published by different research groups. The combined model is robust and it is able to achieve physiological steady-state values, as well as to reproduce the predictions of the individual models. Furthermore, a transition between two versions of our model with new regulatory factors added properly simulates the switch in methionine adenosyl transferase isozymes occurring when the liver enters in proliferative conditions. The combined model is useful to support the previous prediction on the role of S-adenosyl methionine availability in polyamine homeostasis. Furthermore, it could be easily adapted to get deeper insights on the connections of polyamines with energy metabolism. Notes by the author: This model combines BIOMD0000000190 and BIOMD0000000268 from BioModels Database, both models include corrections respect to their originals publications. To simulate a MATI/MATIII switch to MATII in proliferating liver: We set to 0 the Vmax parameters of MATI and MATIII We included MATII reaction equation. We add a regulation factor dependent of SAM levels in ODC and SAMDCe rates of synthesis (66.5/[SAM]). H2O2 was increased in a 50 % according to an initial state ofproliferating and regenerating liver. This model is hosted on BioModels Database and identified by: MODEL1305060001 . To cite BioModels Database, please use: BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models . To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information.

Project description:Reyes-Palomares2012 - a combined model hepatic polyamine and sulfur aminoacid metabolism - version1 Mammalian polyamine metabolism consists of a bi-cycle with two required entrances, omithine and S-adenosyl methionine (SAM), and several alternative exists. The relevant regulatory roles of the short half-life enzymes ornithine decarboxylase (ODC), S-adenosyl methione decarboxylase (SAMDC) and spermindine/spermine acetyl transferase (SSAT) in polyamine metabolism are well studied, and has been modelled here. This model is described in the article: A combined model of hepatic polyamine and sulfur amino acid metabolism to analyze S-adenosyl methionine availability. Reyes-Palomares A, Montañez R, Sánchez-Jiménez F, Medina MA. Amino Acids 2012 Feb; 42(2-3): 597-610 Abstract: Many molecular details remain to be uncovered concerning the regulation of polyamine metabolism. A previous model of mammalian polyamine metabolism showed that S-adenosyl methionine availability could play a key role in polyamine homeostasis. To get a deeper insight in this prediction, we have built a combined model by integration of the previously published polyamine model and one-carbon and glutathione metabolism model, published by different research groups. The combined model is robust and it is able to achieve physiological steady-state values, as well as to reproduce the predictions of the individual models. Furthermore, a transition between two versions of our model with new regulatory factors added properly simulates the switch in methionine adenosyl transferase isozymes occurring when the liver enters in proliferative conditions. The combined model is useful to support the previous prediction on the role of S-adenosyl methionine availability in polyamine homeostasis. Furthermore, it could be easily adapted to get deeper insights on the connections of polyamines with energy metabolism. Notes by the author: This model combines BIOMD0000000190 and BIOMD0000000268 from BioModels Database, both models include corrections respect to their originals publications. This model is hosted on BioModels Database and identified by: BIOMD0000000674. To cite BioModels Database, please use: Chelliah V et al. BioModels: ten-year anniversary. Nucl. Acids Res. 2015, 43(Database issue):D542-8. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information.

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Transcriptome analysis upon Sin3A or Sam-S knockdown or both in Drosophila cultured S2 cells

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