IS911 transpososome assembly as analysed by tethered particle motion

@article{Pouget2006IS911TA,
  title={IS911 transpososome assembly as analysed by tethered particle motion},
  author={No{\"e}lle Pouget and Catherine Turlan and Nicolas Destainville and Laurence Salom{\'e} and Michael Chandler},
  journal={Nucleic Acids Research},
  year={2006},
  volume={34},
  pages={4313 - 4323}
}
Initiation of transposition requires formation of a synaptic complex between both transposon ends and the transposase (Tpase), the enzyme which catalyses DNA cleavage and strand transfer and which ensures transposon mobility. We have used a single-molecule approach, tethered particle motion (TPM), to observe binding of a Tpase derivative, OrfAB[149], amputated for its C-terminal catalytic domain, to DNA molecules carrying one or two IS911 ends. Binding of OrfAB[149] to a single IS911 end… CONTINUE READING

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