Scientist Stories: Jason Chin, Reprogramming the Genetic Code

Jason Chin is currently a Programme Leader at the Medical Research Council Laboratory of Molecular Biology (MRC-LMB), where he is also Head of the Centre for Chemical & Synthetic Biology (CCSB). He is Professor of Chemistry & Chemical Biology at the University of Cambridge, and holds a joint appointment at the University of Cambridge Department of Chemistry. He is also a fellow in Natural Sciences at Trinity College, Cambridge.

Jason is a native of the UK. He was an undergraduate at Oxford University, where he worked with Professor John Sutherland on Cephalosporin biosynthesis. He obtained his PhD as a Fulbright grantee from Yale University, working with Professor Alanna Schepartz. He was a Damon Runyon Fellow at The Scripps Research Institute with Professor Peter Schultz where he developed the first approaches to systematically expand the genetic code of eukaryotic cells and pioneered approaches, that are now widely used, for defining protein interactions by genetically encoding photocrosslinking amino acids.

Jason’s work has been recognized by a number of awards, including: the Francis Crick Prize (Royal Society), the Corday Morgan Prize (Royal Society of Chemistry), European Molecular Biology Organization’s (EMBO) Gold Medal, Louis-Jeantet Young Investigator Career Award, Sackler International Prize in the Physical Science. He is in the European Inventors Hall of Fame, a member of EMBO, a Fellow of the Academy of Medical Sciences, and a Fellow of The Royal Society. His current scientific interests are described in the Research pages.

His lab has pioneered the development and application of methods for reprogramming the genetic code of living organisms. These approaches allow the site specific incorporation of designer unnatural amino acids, beyond the canonical 20, into proteins in diverse cells and organisms.

A fundamental challenge in reprogramming the genetic code of cells is to direct the incorporation of unnatural amino acids into proteins. We have shown that it is possible to create an orthogonal translation pathway in the cell in which a new ribosome, the orthogonal ribosome, is directed to a new message. Since the orthogonal ribosome, unlike the natural ribosome, is not essential it is possible to evolve the orthogonal ribosome to read new genetic codes on the orthogonal message. We have created a ribosome that efficiently reads quadruplet codons and amber codons, that are inefficiently read on the natural ribosome. By directing tRNAs aminoacylated with unnatural amino acids to the orthogonal ribosome we have created a parallel genetic code in the cell. This parallel translation pathway provides a series of blank codons that may be assigned to new amino acids.

We have pioneered the use of pyrrolysyl -tRNA synthetase/tRNA pairs for genetic code expansion. Since we demonstrated that this pair could be evolved for unnatural amino acid incorporation this system has been widely adopted. We continue to investigate and expand the scope of this system for unnatural amino acid incorporation.

We have developed approaches to make proteins bearing post-translational modifications that were previously inaccessible. By investigating the modified recombinant proteins we have created – using structural biology, enzymology and single molecule approaches – we have provided new insight into the role of post-translational modifications, including lysine acetylation, methylation and ubiqutination, in regulating protein structure and biological function.

https://www2.mrc-lmb.cam.ac.uk/group-...

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