Unique contacts direct high-priority recognition of the tetrameric Mu transposase-DNA complex by the AAA plus unfoldase ClpX

被引：30

作者：

Abdelhakim, Aliaa H. ^{[1
]}

Oakes, Elizabeth C. ^{[1
]}

Sauer, Robert T. ^{[1
]}

Baker, Tania A. ^{[1
,2
]}

机构：

[1] MIT, Dept Biol, Cambridge, MA 02139 USA

[2] MIT, Howard Hughes Med Inst, Cambridge, MA 02139 USA

来源：

MOLECULAR CELL | 2008年 / 30卷 / 01期

关键词：

D O I：

10.1016/j.molcel.2008.02.013

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：39 / 50

页数：12

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