Mutagenesis of bacterial elongation factor Tu at lysine 136. A conserved amino acid in GTP regulatory proteins.

@article{Hwang1989MutagenesisOB,
  title={Mutagenesis of bacterial elongation factor Tu at lysine 136. A conserved amino acid in GTP regulatory proteins.},
  author={Yu Wen Hwang and Ana Ureba S{\'a}nchez and Daniel L Miller},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 14},
  pages={8304-9}
}
We have studied the effects of specific amino acid replacements in EF-Tu upon the protein's interactions with guanine nucleotides and elongation factor Ts (EFTs). We found that alterations at the lysine residue of the Asn-Lys-Cys-Asp sequence, the guanine ring-binding sequence, differentially affect the protein's ability to bind guanine nucleotides. Wild type EF-Tu (Lys-136) binds GDP and GTP much more tightly than do many of the altered proteins. Replacing lysine by arginine lowers the protein… CONTINUE READING

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