RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli.

@article{Anton2008RimOAM,
  title={RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli.},
  author={Brian P. Anton and Lana Saleh and Jack S. Benner and Elisabeth A Raleigh and Simon Kasif and R. J. Roberts},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2008},
  volume={105 6},
  pages={1826-31}
}
Ribosomal protein S12 undergoes a unique posttranslational modification, methylthiolation of residue D88, in Escherichia coli and several other bacteria. Using mass spectrometry, we have identified the enzyme responsible for this modification in E. coli, the yliG gene product. This enzyme, which we propose be called RimO, is a radical-S-adenosylmethionine protein that bears strong sequence similarity to MiaB, which methylthiolates tRNA. We show that RimO and MiaB represent two of four subgroups… CONTINUE READING