The 26S proteasome of the lignin-degrading Basidiomycete Phlebia radiata

摘要: Abstract The 26S proteasome, a large multicatalytic protease complex is involved in highly selective ATP-dependent degradation of intracellular proteins eukaryotes, typically those tagged with polyubiquitin chain. proteasome-mediated proteolysis plays key role the regulation critical cellular processes such as transcriptional control, cell cycle progression, and stress response. Biochemical structural properties proteasomes described this paper concern white-rot fungus Phlebia radiata , which interesting from standpoint biotechnological applications ligninolytic enzymes. In addition, characterization P. belongs to class Basidiomycetes first one reported kingdom fungi for an organism other than yeast representing Ascomycetes. All distinct peptidase activities: chymotrypsin-, trypsin-, caspase-like attributed were detected proteasome preparations. Electrophoretic mobility, subunit composition, ATP-dependence, sensitivity proteasome-specific inhibitors, inactivation by low concentrations SDS demonstrated these preparations are typical features species. Moreover, findings vivo blocking function strongly support previous interpretation that proteasomal pathway activity some enzymes under nutrient deprivation [Staszczak M. Proteasomal pathways Trametes versicolor . Enzyme Microb Technol 2002;30:537–41].