Targeted and proximity-dependent promiscuous protein biotinylation by a mutant Escherichia coli biotin protein ligase.

@article{Cronan2005TargetedAP,
  title={Targeted and proximity-dependent promiscuous protein biotinylation by a mutant Escherichia coli biotin protein ligase.},
  author={John E. Cronan},
  journal={The Journal of nutritional biochemistry},
  year={2005},
  volume={16 7},
  pages={416-8}
}
  • John E. Cronan
  • Published 2005 in The Journal of nutritional biochemistry
A method for general protein biotinylation by enzymatic means has been developed. A mutant form (R118G) of the biotin protein ligase (BirA) of Escherichia coli is used and biotinylation is thought to proceed by chemical acylation of protein lysine side chains by biotinoyl-5'-AMP released from the mutant protein. Bovine serum albumin, chloramphenicol acetyltransferase, immunoglobulin chains and RNAse A as well as a large number of E. coli proteins have been biotinylated. The biotinylation… CONTINUE READING