The filamentous fungus Trichoderma reesei is one of the most efficient eukaryotic cell factories available. Considering its extraordinary secretion capacity, this species can be characterised as “a professional” protein secretor. Protein quality control is a crucial cellular function. Proteins that are not folded correctly or not fully assembled are recognised in the early secretory pathway and subjected to degradation by the ubiquitin-proteasome pathway featuring a large (approximately 2.5 MDa) multicatalytic protease, the proteasome. The proteolysis of cellular proteins is a highly complex, temporally controlled and tightly regulated process. An isolation method for the 20S proteasome of T. reesei and a 2D master map of the fungal proteasome have been established. From the map, a number of proteasome subunit proteins as well as proteasome-interacting proteins have been identified. We are also in the process of creating a series of mutant forms of the main cellobiohydrolase enzyme CBHI to trace its secretion and presumed degradation in the proteasome.
|Number of pages||1|
|Publication status||Published - 2006|
|Event||European Conference on Fungal Genetics (8th : 2006) - Vienna, Austria|
Duration: 8 Apr 2006 → 11 Apr 2006
|Conference||European Conference on Fungal Genetics (8th : 2006)|
|Period||8/04/06 → 11/04/06|