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pmid:27547807

Ovary and embryo proteogenomic dataset revealing diversity of vitellogenins in the crustacean Gammarus fossarum.

Judith Trapp · Jean-Charles Gaillard · Arnaud Chaumot · Olivier Geffard · Olivier Pible · Jean Armengaud

Data in brief · 2016 doi:10.1016/j.dib.2016.07.045

Paper

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Ovary and embryo proteogenomic dataset revealing diversity of vitellogenins in the crustacean Gammarus fossarum.
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10.1016/j.dib.2016.07.045
pmid
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Judith Trapp
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Jean-Charles Gaillard
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Arnaud Chaumot
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Olivier Geffard
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Jean Armengaud
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Data in brief
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2016
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Ovaries and embryos from sexually mature Gammarus fossarum were sampled at different stages of the reproductive cycle. The soluble proteome was extracted for five biological replicates and samples were subjected to trypsin digestion. The resulting peptides were analyzed by high resolution tandem mass spectrometry with a LTQ-Orbitrap XL instrument. The MS/MS spectra were assigned with a previously described RNAseq-derived G. fossarum database. The proteins highlighted by proteogenomics were monitored and their abundance kinetics over the different stages revealed a large panel of vitellogenins. Criteria were i) accumulation during oogenesis, ii) decrease during embryogenesis, iii) classified as female-specific, and iv) sequence similarity and phylogenetic analysis. The data accompanying the manuscript describing the database searches and comparative analysis ("High-throughput proteome dynamics for discovery of key proteins in sentinel species: unsuspected vitellogenins diversity in the crustacean Gammarus fossarum" by Trapp et al. [1]) have been deposited to the ProteomeXchange via the PRIDE repository with identifiers PRIDE: PXD001002.
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Proteins were extracted and analyzed by shotgun proteogenomics. Five biological replicates were performed for each stage. Five molt stages were analyzed: post-molt stage A and B, inter-molt stage C1, inter-molt stage C2, pre-molt stage D1, and pre-molt stage D2. Accordingly, five different embryo development stages were analyzed."], ["Experimental features", "The 50 soluble protein extracts were briefly run on SDS-PAGE, followed by in-gel trypsin proteolysis. 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