Gene dissection demonstrates that the Escherichia coli cysG gene encodes a multifunctional protein.

@article{Warren1994GeneDD,
  title={Gene dissection demonstrates that the Escherichia coli cysG gene encodes a multifunctional protein.},
  author={Martin J. Warren and Edward L. Bolt and Charles A. Roessner and A. I. Scott and Jonathan B. Spencer and Sarah C. Woodcock},
  journal={The Biochemical journal},
  year={1994},
  volume={302 ( Pt 3)},
  pages={837-44}
}
The C-terminus of the Escherichia coli CysG protein, consisting of amino acids 202-457, was expressed as a recombinant protein using gene dissection methodology. Analysis of the activity of this truncated protein, termed CysGA, revealed that it was able to methylate uroporphyrinogen III in the same S-adenosyl-L-methionine (SAM)-dependent manner as the complete CysG protein. However, this truncated protein was not able to complement E. coli cysG cells, thereby suggesting that the first 201 amino… CONTINUE READING