A conserved inter-domain communication mechanism regulates the ATPase activity of the AAA-protein Drg1.

ABSTRACT: AAA-ATPases fulfil essential roles in different cellular pathways and often act in form of hexameric complexes. Interaction with pathway-specific substrate and adaptor proteins recruits them to their targets and modulates their catalytic activity. This substrate dependent regulation of ATP hydrolysis in the AAA-domains is mediated by a non-catalytic N-terminal domain. The exact mechanisms that transmit the signal from the N-domain and coordinate the individual AAA-domains in the hexameric complex are still the topic of intensive research. Here, we present the characterization of a novel mutant variant of the eukaryotic AAA-ATPase Drg1 that shows dysregulation of ATPase activity and altered interaction with Rlp24, its substrate in ribosome biogenesis. This defective regulation is the conseq

SUBMITTER: Prattes M 

PROVIDER: S-EPMC5356007 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature