La Jolla, CA, April 20, 2001 Scientists at The Skaggs Institute for Chemical Biology at The Scripps Research Institute (TSRI), have published two separate papers in the current issue of the journal Science in which they describe two different ways of engineering bacterial cells to encode "unnatural" proteins.
These proteins differ from those produced by other living organisms because they incorporate novel amino acids, the subunit molecules of which proteins are composed.
Both of these methods could provide powerful new mechanisms for studying protein and cellular functions, because they are proof-of-principal that bacterial strains can be made to incorporate novel amino acids into proteins. In addition, they could enable scientists to envision the possibility of engineering completely new proteins.
According to TSRI President Richard A. Lerner, M.D., "One of the holy grails of modern genetics is the extension of the genetic code to increase the ability of proteins to perform new chemical tasks. We at The Skaggs Institute of TSRI are extremely proud to have accomplished this by two separate routes."
Principal Investigators Peter Schultz, Ph.D., Scripps Family Chair, The Skaggs Institute and Department of Chemistry; and Paul Schimmel, Ph.D., Ernest and Jean Hahn Professor and Chair, The Skaggs Institute, and Departments of Molecular Biology and Chemistry, led the two separate efforts.
The research article, "Enlarging the Amino Acid Set of Escherichia coli by Infiltrating the Valine Coding Pathway," is authored by Volker Dring, Henning D. Mootz, Leslie A. Nangle, Tamara L. Hendrickson, Valrie de Crcy-Lagard, Paul Schimmel, and Philippe Marlire.
The research article, "Expanding the Genetic Code of Escherichia coli," is authored by Lei Wang, Ansgar Brock, Brad Herberich, and Peter G. Schultz.
Encoding proteins from DNA is one of the most fundamental requirements for life, since proteins do much of the microscopic work of the cell a
Contact: Robin B. Goldsmith
Scripps Research Institute