ProjectDas Proteom und Interaktom des Glykogenstoffwechselapparates
Basic data
Title:
Das Proteom und Interaktom des Glykogenstoffwechselapparates
Duration:
01/01/2019 to 31/12/2021
Abstract / short description:
Proteome and interactome of the glycogen metabolism apparatus
Global detection and quantification of proteome dynamics is one of the fundamental requirements for understanding molecular processes on a systems level. In close collaboration with other members of the SCyCode consortium, we will determine the proteome and interactome of the glycogen granules in the model cyanobacterium Synechocystis sp. PCC 6803, and study its dynamics under different conditions of glycogen accumulation or degradation. We will extend these analyses to a quantitative phosphoproteomic screen of all known serine/threonine kinases and phosphatases of Synechocystis to identify their potential substrates under different conditions of glycogen accumulation. Finally, we will develop a protocol based on protein correlation profiling after density gradient centrifugation to address subcellular localization and composition of enzyme complexes involved in glycogen metabolism and sugar catabolism and apply it to study spatial and temporal dynamics of protein complexes during heterotrophy-autotrophy (glycolytic-glyconeogenetic) switches. Taken together, this project will reveal the full protein composition of the glycogen granules and the protein interaction network related to regulation of glycogen metabolism; decipher the first kinase/phosphatase substrate network in Cyanobacteria and its involvement in regulation of glycogen metabolism; define the first spatially resolved proteome of a Cyanobacterium and enable detection of previously unknown protein-protein and protein-RNA complexes involved in regulation of glycogen metabolism.
Global detection and quantification of proteome dynamics is one of the fundamental requirements for understanding molecular processes on a systems level. In close collaboration with other members of the SCyCode consortium, we will determine the proteome and interactome of the glycogen granules in the model cyanobacterium Synechocystis sp. PCC 6803, and study its dynamics under different conditions of glycogen accumulation or degradation. We will extend these analyses to a quantitative phosphoproteomic screen of all known serine/threonine kinases and phosphatases of Synechocystis to identify their potential substrates under different conditions of glycogen accumulation. Finally, we will develop a protocol based on protein correlation profiling after density gradient centrifugation to address subcellular localization and composition of enzyme complexes involved in glycogen metabolism and sugar catabolism and apply it to study spatial and temporal dynamics of protein complexes during heterotrophy-autotrophy (glycolytic-glyconeogenetic) switches. Taken together, this project will reveal the full protein composition of the glycogen granules and the protein interaction network related to regulation of glycogen metabolism; decipher the first kinase/phosphatase substrate network in Cyanobacteria and its involvement in regulation of glycogen metabolism; define the first spatially resolved proteome of a Cyanobacterium and enable detection of previously unknown protein-protein and protein-RNA complexes involved in regulation of glycogen metabolism.
Keywords:
Proteomics
Caanobacteria
Gylcogen
Mass spectrometry (Massenspektrometrie)
Metabolism (Metabolismus)
Involved staff
Managers
Faculty of Science
University of Tübingen
University of Tübingen
Department of Biology
Faculty of Science
Faculty of Science
Local organizational units
Quantative Proteomics
Interfaculty Institute for Cell Biology (IFIZ)
Interfaculty Institutes
Interfaculty Institutes
Funders
Bonn, Nordrhein-Westfalen, Germany