PMID:18406325

Citation	Abdelhakim, AH, Oakes, EC, Sauer, RT and Baker, TA (2008) Unique contacts direct high-priority recognition of the tetrameric Mu transposase-DNA complex by the AAA+ unfoldase ClpX. Mol. Cell 30:39-50
Abstract	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.
Links	PubMed PMC2717000 Online version:10.1016/j.molcel.2008.02.013
Keywords	ATPases Associated with Diverse Cellular Activities; Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Amino Acid Substitution; Binding Sites; DNA/chemistry; DNA/metabolism; Endopeptidase Clp/chemistry; Endopeptidase Clp/genetics; Endopeptidase Clp/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Macromolecular Substances/chemistry; Macromolecular Substances/metabolism; Models, Molecular; Molecular Chaperones/chemistry; Molecular Chaperones/genetics; Molecular Chaperones/metabolism; Point Mutation; Protein Binding; Protein Structure, Quaternary; Transposases/chemistry; Transposases/genetics; Transposases/metabolism
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BPMU:TRA	part_of	GO:0018995: host	ECO:0000315: mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
BPMU:TNPA	part_of	GO:0018995: host	ECO:0000315: mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete

References

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