The molecular structure of wild-type and a mutant Fis protein: relationship between mutational changes and recombinational enhancer function or DNA binding.

@article{Yuan1991TheMS,
  title={The molecular structure of wild-type and a mutant Fis protein: relationship between mutational changes and recombinational enhancer function or DNA binding.},
  author={Huidong Yuan and Steven E. Finkel and Jiawen Feng and Maria Kaczor-Grzeskowiak and Reid C. Johnson and Richard E. Dickerson},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1991},
  volume={88 21},
  pages={9558-62}
}
The 98-amino acid Fis protein from Escherichia coli functions in a variety of reactions, including promotion of Hin-mediated site-specific DNA inversion when bound to an enhancer sequence. It is unique among site-specific DNA-binding proteins in that it binds to a large number of different DNA sequences, for which a consensus sequence is difficult to… CONTINUE READING