Disassembly of the Mu transposase tetramer by the ClpX chaperone.

@article{Levchenko1995DisassemblyOT,
  title={Disassembly of the Mu transposase tetramer by the ClpX chaperone.},
  author={I. A. Levchenko and Lusong Luo and Tania A. Baker},
  journal={Genes & development},
  year={1995},
  volume={9 19},
  pages={2399-408}
}
Mu transposition is promoted by an extremely stable complex containing a tetramer of the transposase (MuA) bound to the recombining DNA. Here we purify the Escherichia coli ClpX protein, a member of a family of multimeric ATPases present in prokaryotes and eukaryotes (the Clp family), on the basis of its ability to remove the transposase from the DNA after recombination. Previously, ClpX has been shown to function with the ClpP peptidase in protein turnover. However, neither ClpP nor any other… CONTINUE READING

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