Proteomic profiling of mitochondrial protein networks
Our knowledge of basic cellular processes is largely deduced from studies on a small number of model proteins. From these analyses general conclusions were drawn on how proteins are synthesized, sorted between cellular compartments, folded, assembled into oligomeric structures and degraded by proteolysis. However, recent observations showed that many proteins do not strictly follow these general schemes but rather use individual biogenesis pathways. These can be variations of, but also even complete deviations from, classical biogenesis pathways.
In this project we will employ unbiased proteome-wide methods to explore protein biogenesis more generally. This strategy is accompanied by a comprehensive biochemical characterization of individual proteins which show deviations from general biogenesis pathways. Moreover, we will use these proteome-wide data to evaluate how generally common cell biological concepts apply and, if applicable, to modify these concepts accordingly. The experimental system used in this project are mitochondrial protein networks in yeast since this allows us to make use of the comprehensive knowledge that exists on the function and physical interactions of these proteins. This interdisciplinary project relies on the close cooperation of groups specialized in different fields, in particular yeast genetics, mitochondrial biology and biochemistry (Herrmann), proteomics (Schroda) and informatics (Garth, NN).