Sir Richard J. Roberts, Ph.D.

Director/Scientific Advisory Board
Compensation Committee (Member)
Nominating and Corporate Governance Committee (Member)

Sir Richard J. Roberts won the 1993 Nobel Prize in Medicine and Physiology. He is the Chief Scientific Officer at New England Biolabs, Ipswich, Massachusetts. He was educated in England, attending St. Stephen’s School and the City of Bath Boys’ School in Bath before moving to the University of Sheffield, where he obtained a BSc in Chemistry in 1965 and a Ph.D. in Organic Chemistry in 1968. His postdoctoral research was carried out in Professor J.L. Strominger’s laboratory at Harvard, where he studied the tRNAs that are involved in the biosynthesis of bacterial cell walls. From 1972 to 1992 he worked at Cold Spring Harbor Laboratory, reaching the position of Assistant Director for Research under Dr. J.D. Watson.

Sir Richard’s current research interests focus on using bioinformatics and genomics to find new enzyme activities and to drive his experimental program. Most recently he is involved in a large community-based project called COMBREX aimed at improving the functional annotation of genomes. He began work on the newly discovered Type II restriction enzymes in 1972 and in the next few years more than 100 such enzymes were discovered and characterized in Sir Richard’s laboratory. His laboratory has cloned the genes for several restriction enzymes and their cognate methylases, and study of these enzymes has been a major research theme. Sir Richard has also been involved in studies of Adenovirus-2, beginning with studies of transcription that led to the discovery of split genes and mRNA splicing in 1977. This was followed by efforts to deduce the DNA sequence of the Adenovirus-2 genome; a complete sequence of 35,937 nucleotides was obtained. This latter project required the extensive use of computer methods, both for the assembly of the sequence and its subsequent analysis. His laboratory pioneered the application of computers in this area, and the further development of computer methods of protein and nucleic acid sequence analysis continues to be a major research focus. The field of DNA methyltransferases is also an area of active research interest, and crystal structures for the HhaI methyltransferase, both alone and in complex with DNA, have been obtained in collaboration with Dr. X. Cheng. The latter complex is quite remarkable as the protein causes the target cytosine base to flip completely out of the helix, so that it is clear that there are many more restriction enzyme genes in nature than had been previously suspected.