Project description:The larval ovary is made up of multiple cell types including germ cells and somatic cells. The diversity of cell types and transcriptional regulation is not fully understood. To get single cell resolution of larval ovary regulation, we generated single-cell RNA expression profiles (scRNA-Seq) from late third instar larval ovaries of a reference Drosophila melanogaster genotype w[1118].
Project description:RNA-seq on Drosophila melanogaster ovary (stages 1-7) in: diapause at 12ºC (after 28 days), reproductive at 12ºC (after 28 days), and age-matched control at 25ºC in two inbred genotypes. Each biological replicate is a pool of 25 ovary pairs, and each treatment has three biological replicates.
Project description:Insect ovaries are made up of tubular egg producing subunits called ovarioles, whose number largely determines the number of eggs that can be potentially laid. Ovariole number is directly determined by the number of cellular structures called terminal filaments, which are stacks of cells that assemble in the larval ovary. Elucidating the developmental and regulatory mechanisms of terminal filament formation is thus key to understanding the regulation of insect reproduction through ovariole number regulation. We systematically measured mRNA expression of all cells in the Drosophila larval ovary at the beginning, middle and end of terminal filament formation using RNA-seq. We also separated somatic and germ line cells during these stages and assessed their tissue-specific gene expression during larval ovary development.
Project description:We report the proteome composition of the Drosophila eye – a compound organ that is highly enriched in membrane proteins. The fly eye is a popular model to study the physiology of vision by means of genetic, pharmacological, and dietary interference.While the eye transcriptome and development-related changes of gene expression profiles have been extensively studied, little is known about the eye proteome.we employed GeLC-MS/MS to identify and rank the abundances of 3516 eye proteins. Moreover, we applied our MS Western method to determine the absolute (molar) abundances of a related set of proteins that are important for photoreceptor structure (including maintenance) and function (phototransduction). Altogether, we provide a comprehensive and expandable proteomics resource that will be valuable for a variety of studies of ocular biochemistry, physiology, and development.