Structural basis of aggregate binding by the AAA+ disaggregase ClpG.

ABSTRACT: Severe heat stress causes massive loss of essential proteins by aggregation, necessitating a cellular activity that rescues aggregated proteins. This activity is executed by ATP-dependent, ring-forming, hexameric AAA+ disaggregases. Little is known about the recognition principles of stress-induced protein aggregates. How can disaggregases specifically target aggregated proteins, while avoiding binding to soluble non-native proteins? Here, we determined by NMR spectroscopy the core structure of the aggregate-targeting N1 domain of the bacterial AAA+ disaggregase ClpG, which confers extreme heat resistance to bacteria. N1 harbors a Zn²⁺-coordination site that is crucial for structural integrity and disaggregase functionality. We found that conserved hydrophobic N1 residues locate

SUBMITTER: Katikaridis P 

PROVIDER: S-EPMC10641755 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature