Functional interactions between the MutL and Vsr proteins of Escherichia coli are dependent on the N-terminus of Vsr.

@article{Monastiriakos2004FunctionalIB,
  title={Functional interactions between the MutL and Vsr proteins of Escherichia coli are dependent on the N-terminus of Vsr.},
  author={Stavroula K Monastiriakos and Kathy M J Doiron and Marina I. Siponen and Claire G. Cupples},
  journal={DNA repair},
  year={2004},
  volume={3 6},
  pages={639-47}
}
The crystal structure of the Escherichia coli Vsr endonuclease bound to a C(T/G)AGG substrate revealed that the DNA is held by a pincer composed of a trio of aromatic residues which intercalate into the major groove, and an N-terminus alpha helix which lies across the minor groove. We have constructed an N-terminus truncation (Delta14) which removes most of the alpha helix. The mutant is still fairly proficient in mediating very short patch repair. However, its endonuclease activity is… CONTINUE READING