The AddAB helicase/nuclease forms a stable complex with its cognate chi sequence during translocation.

@article{Chedin2006TheAH,
  title={The AddAB helicase/nuclease forms a stable complex with its cognate chi sequence during translocation.},
  author={Frederic Chedin and Naofumi Handa and Mark S Dillingham and Stephen C Kowalczykowski},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 27},
  pages={18610-7}
}
The Bacillus subtilis AddAB enzyme possesses ATP-dependent helicase and nuclease activities, which result in the unwinding and degradation of double-stranded DNA (dsDNA) upon translocation. Similar to its functional counterpart, the Escherichia coli RecBCD enzyme, it also recognizes and responds to a specific DNA sequence, referred to as Chi (chi). Recognition of chi triggers attenuation of the 3'- to 5'-nuclease, which permits the generation of recombinogenic 3'-overhanging, single-stranded… CONTINUE READING
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Stable Binding of AddAB Enzyme to 18616 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME

  • M.G, P. Bessieres, +16 authors A Danchin
  • JULY
  • 2006

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