Project description:Characterization of the riboproteome composition in quiescent cells and post-translational reactivation. To characterize ribosome heterogeneity during the exit from quiescence, the protein composition of ribosomal particles from stationary phase and nutrient-stimulated cells was assessed. A label-free quantitative mass spectrometry strategy was taken to compare quiescent yeast cells with cells that had been nutrient stimulated for 30 and 60 min. To this end, crude extracts from these cells were subjected to sucrose gradient centrifugation and three fractions free (F); monosome (M=80S + 60S + 40S) and polysome (P) were analyzed by nano-HPLC-MS/MS. A total of 528 proteins were identified.
Project description:MS/MS data obtained from crude extracts from Pseudoalteromonas sp. This data is not publisher yet, so, contact Mr. Christian Martin before use it.
Project description:We investigated the effects of SAICAR accumulation on transcriptional regulation of purine biosynthesis and other metabolic pathways. These data were compared to those obtained in the ade16ade17 vs WT comparison to determine the effects associated to accumulation of SAICAR alone. In this work, global transcription analyses were combined to measurements of intracellular nucleotides pools by HPLC. Keywords: Comparative genomic transcription analysis on total RNA from cells accumulating or not SAICAR.
Project description:LC-MS/MS analysis of promoter pull-down assays with crude protein extracts from R. eutropha Re2058/pCB113, to identify putative transcriptional regulators involved in the expression control of PHA metabolism, specifically targeting phasin phaP1 and depolymerase phaZ3 and phaZ5 genes.
Project description:Hydrophilic interaction liquid chromatography coupled with LC- MS/MS was used to analyze the crude venom extracts of Echis ocellatus (Carpet viper) and Bitis arietans (Puff adder). The gel-free proteomic analysis of the crude venom extracts from E. ocellatus and B. arietans yielded the identification of 86 and 80 proteins, respectively. Seventy- nine proteins were common between the two snake species with a 90.8% similarity. The identified proteins belong to 12 protein families where serine proteases (22.31%) and metalloproteinases (21.06%) were the dominant proteins in the venom of B. arietans. Metalloproteinases (34.84%), phospholipase A 2 s (25.69%) and serine proteases (17.25%) represents the major toxins in the E. ocellatus venom. This study provides some valuable insights into the toxin families to be neutralized in case of envenomation.