The proteasome activity reporter GFP-Cl1 is degraded by autophagy in the aging model Podospora anserina.

ABSTRACT: The degradation of damaged proteins is an important vital function especially during aging and stress. The ubiquitin proteasome system is one of the major cellular machineries for protein degradation. Health and longevity are associated with high proteasome activity. To demonstrate such a role in aging of Podospora anserina, we first analyzed the transcript and protein abundance of selected proteasome components in wild-type cultures of different age. No significant differences were observed. Next, in order to increase the overall proteasome abundance we generated strains overexpressing the catalytic proteasome subunits PaPRE2 and PaPRE3. Although transcript levels were strongly increased, no substantial effect on the abundance of the corresponding proteins was observed. Finally, the analy

SUBMITTER: Wiemer M 

PROVIDER: S-EPMC4264638 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature