Characterisation of the Trichoderma reesei proteasome

Liisa K. Kautto, Jasmine Grinyer, Peter L. Bergquist, V. S. Junior Te'o, K. M. Helena Nevalainen

Research output: Contribution to conferenceAbstract


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.
Original languageEnglish
Number of pages1
Publication statusPublished - 2006
EventEuropean Conference on Fungal Genetics (8th : 2006) - Vienna, Austria
Duration: 8 Apr 200611 Apr 2006


ConferenceEuropean Conference on Fungal Genetics (8th : 2006)
CityVienna, Austria

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