한빛사 논문
Minseob Koh,†,# Anzhi Yao,†,# Patrick R. Gleason,‡ Jeremy H. Mills,‡ and Peter G. Schultz*,†
† Department of Chemistry and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, United States
‡ School of Molecular Sciences and The Biodesign Center for Molecular Design and Biomimetics, Arizona State University, Tempe, Arizona 85281, United States
*Corresponding Author
Author Contributions
#M.K. and A.Y. contributed equally.
Abstract
Synthetic auxotrophy in which bacterial viability depends on the presence of a synthetic amino acid provides a robust strategy for the containment of genetically modified organisms and the development of safe, live vaccines. However, a simple, general strategy to evolve essential proteins to be dependent on synthetic amino acids is lacking. Using a temperature-sensitive selection system, we evolved an Escherichia coli (E. coli) sliding clamp variant with an orthogonal protein–protein interface, which contains a Leu273 to p-benzoylphenyl alanine (pBzF) mutation. The E. coli strain with this variant DNA clamp has a very low escape frequency (<10–10), and its growth is strictly dependent on the presence of pBzF. This selection strategy can be generally applied to create ncAA dependence of other organisms with DNA clamp homologues.
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