Ontology highlight
ABSTRACT:
SUBMITTER: Abdelhakim AH
PROVIDER: S-EPMC2717000 | biostudies-literature | 2008 Apr
REPOSITORIES: biostudies-literature
Abdelhakim Aliaa H AH Oakes Elizabeth C EC Sauer Robert T RT Baker Tania A TA
Molecular cell 20080401 1
Clp/Hsp100 ATPases remodel and disassemble multiprotein complexes, yet little is known about how they preferentially recognize these complexes rather than their constituent subunits. We explore how substrate multimerization modulates recognition by the ClpX unfoldase using a natural substrate, MuA transposase. MuA is initially monomeric but forms a stable tetramer when bound to transposon DNA. Destabilizing this tetramer by ClpX promotes an essential transition in the phage Mu recombination path ...[more]