N-terminal acetylation and replicative age affect proteasome localization and cell fitness during aging.

ABSTRACT: Specific degradation of proteins is essential for virtually all cellular processes and is carried out predominantly by the proteasome. The proteasome is important for clearance of damaged cellular proteins. Damaged proteins accumulate over time and excess damaged proteins can aggregate and induce the death of old cells. In yeast, the localization of the proteasome changes dramatically during aging, possibly in response to altered proteasome activity requirements. We followed two key parameters of this process: the distribution of proteasomes in nuclear and cytosolic compartments, and the formation of cytoplasmic aggregate-like structures called proteasome storage granules (PSGs). Whereas replicative young cells efficiently relocalized proteasomes from the nucleus to the cytoplasm and forme

SUBMITTER: van Deventer S 

PROVIDER: S-EPMC4282048 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature