Protein targeting and safeguarding upon oxidative unfolding stress (B07)

Oxidative stress causes the generation of mis- and unfolded proteins due to decline in fidelity of mRNA and protein biosynthesis and oxidative damage of proteins. The concomitant drop in cellular ATP level poses a particular hazardous situation for the cell, which leads to the activation of ATP-independent chaperones. Here, we will study the cytosolic targeting factor ASNA1 which switches into a general ATP-independent chaperone upon oxidative stress and explore its crosstalk with cellular proteostasis systems as a downstream mechanism to prevent potentially toxic protein aggregation in HEK293 cells and C. elegans.

DFG Programme Collaborative Research Centres

Subproject of SFB 1678:  Systems-level consequences of fidelity changes in mRNA and protein biosynthesis

Applicant Institution Universität zu Köln

Project Head Professorin Dr. Kathrin Ulrich