期刊
MOLECULAR CELL
卷 30, 期 1, 页码 39-50出版社
CELL PRESS
DOI: 10.1016/j.molcel.2008.02.013
关键词
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资金
- Howard Hughes Medical Institute Funding Source: Medline
- NIAID NIH HHS [AI-16892, R01 AI016892-30, R01 AI016892] Funding Source: Medline
- NIGMS NIH HHS [R01 GM049224-17, R01 GM049224, GM-49224] Funding Source: Medline
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 pathway. We show that ClpX interacts more tightly with tetrameric than with monomeric MuA. Residues exposed only in the MuA tetramer are important for enhanced recognition-which requires the N domain of ClpX-as well as for a high maximal disassembly rate. We conclude that an extended set of potential enzyme contacts are exposed upon assembly of the tetramer and function as internal guides to recruit ClpX, thereby ensuring that the tetrameric complex is a high-priority substrate.
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