Unknown,Transcriptomics,Genomics,Proteomics

Dataset Information

Transcription profiling of Drosophila Spargel mutant versus genetically matched wildtype control

ABSTRACT: Mammalian PGC-1alpha, PGC-1beta and PRC are structurally related transcriptional coactivators, and are involved in multiple metabolic functions, including the regulation of mitochondrial biogenesis. However, due to redundancy, their in vivo roles are still poorly understood. By a genome-wide microarray study, we show that in the Drosophila larval fat body, Spargel (CG9809), the only fly PGC-1 family homologue, is required for proper expression of multiple genes encoding mitochondrial proteins. Experiment Overall Design: Six samples were analyzed in total: three biological replicates of the control (wt) and three biological replicates of the mutant (KG).

ORGANISM(S): Drosophila melanogaster

SUBMITTER: Stefanie Tiefenboeck

PROVIDER: E-GEOD-14780 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

ACCESS DATA

Publications

The Drosophila PGC-1 homologue Spargel coordinates mitochondrial activity to insulin signalling.

Tiefenböck Stefanie K SK Baltzer Claudia C Egli Nicole A NA Frei Christian C

The EMBO journal 20091112 1

Mitochondrial mass and activity must be adapted to tissue function, cellular growth and nutrient availability. In mammals, the related transcriptional coactivators PGC-1alpha, PGC-1beta and PRC regulate multiple metabolic functions, including mitochondrial biogenesis. However, we know relatively little about their respective roles in vivo. Here we show that the Drosophila PGC-1 family homologue, Spargel, is required for the expression of multiple genes encoding mitochondrial proteins. Accordingl ...[more]

PMID: 19910925

Similar Datasets

Project description:Resistance of Saccharomyces cerevisiae to high furfural concentration is based on NADPH-dependent reduction by at least two oxireductases. Biofuels derived from lignocellulosic biomass hold promises for a sustainable fuel economy, but several problems hamper their economical feasibility. One important problem is the presence of toxic compounds in processed lignocellulosic hydrolysates with furfural as a key toxin. While Saccharomyces cerevisiae has some intrinsic ability to reduce furfural to the less toxic furfuryl alcohol, higher resistance is necessary for process conditions. By comparing an evolved, furfural resistant strain and its parent in micro-aerobic, glucose-limited chemostats at increasing furfural challenge, we elucidate key mechanism and the molecular basis of both natural and high-level furfural resistance. At lower furfural concentrations, NADH-dependent oxireductases are the main defence mechanism. At concentrations above 15 mM, however, [1-13C]-flux and global array-based transcript analysis demonstrated that the NADPH-generating flux through pentose-phosphate pathway increases and that NADPH-dependent oxireductases became the major resistance mechanism. The transcript analysis further revealed that iron transmembrane transport is up-regulated in response to furfural. While these responses occur in both strains, high-level resistance in the evolved strain was based on strong induction of ADH7, the uncharacterised ORF YKL071W and 4 further, likely NADPH-dependent oxireductases. By overexpressing the ADH7 gene and the ORF YKL071W, we inverse engineered significantly increased furfural resistance in the parent strain, thereby demonstrating these two enzymes to be key elements of the resistance phenotype. Experiment Overall Design: RNA levels were measured in glucose limited, micro-aerobic chemostat cultures with different concentrations of the growth inhibitor furfural. Two strains were compared: TMB3400-FT30-3 is a strain that has been evolutionary adapted to withstand high furfural concentrations. TMB3400 is its less resistant parent. Number of biological replicates: 2-3.

Dataset Information

Transcription profiling of Drosophila Spargel mutant versus genetically matched wildtype control

Publications

The Drosophila PGC-1 homologue Spargel coordinates mitochondrial activity to insulin signalling.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets