
Sir Richard Roberts (center) with LSBI Associate Director Daniel Peterson (left) and LSBI Director Shane Burgess (right)
SIR RICHARD J. ROBERTS, Ph.D.
1993 Nobel Prize winner for discovery of the discontinuous
nature of eukaryotic genes (exons and introns)
Pioneer in restriction enzyme biochemistry and computational biology
Chief Scientific Officer, New England BioLabs
Discussion with students in Genomes & Genomics
Date: November 4, 2008
Time: 12:30 PM - 1:30 PM
Dr. Roberts spent an hour discussing science, politics, etc., with students
in Dr. Peterson's Genomes & Genomics course.
Seminar 1
Date: November 4, 2008
Time: 2:00 PM - 3:00 PM
Place: Swalm Chemical Engineering
Auditorium
Topic: Dr. Roberts discussed his work at
New England BioLabs (NEB),
a highly-successful corporation with an unparalleled commitment to basic scientific
research, social/fiscal responsibility, and environmental stewardship.
Sponsored by the
Jack Hatcher Entrepreneurship Program and the
Life Sciences & Biotechnology Institute
Photos:
Seminar 2
Date: November 4, 2008
Time: 3:30 PM - 4:30 PM
Place:
Franklin
Center for Furniture Manufacturing and Management, Franklin Auditorium
Topic: Dr. Roberts discussed his groundbreaking work on the molecular evolution
of restriction enzyme/modification systems.
Notes: The talk will be followed by refreshments in the Franklin showroom
Sponsored by the Life Sciences
& Biotechnology Institute and the
Jack Hatcher Entrepreneurship Program
About Dr. Roberts
Dr. Richard J. Roberts is the Chief Scientific Officer at
New England BioLabs, Beverly, 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 B.Sc. 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. James D. Watson.
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 Dr. Roberts' laboratory. His laboratory has cloned the genes for several
restriction enzymes and their cognate methylases, and studies of these enzymes
has been a major research theme. Dr. Roberts 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 for which he was later
awarded a Nobel Prize in Medicine/Physiology. This was followed by efforts
to deduce the DNA sequence of the Adenovirus-2 genome and 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 accessible for chemical reaction. This extreme, but
elegant, distortion of the double helix had not been seen previously. A consuming
interest at present is the semi-automatic identification of restriction enzyme
and methylase genes within the GenBank database and the development of rapid
methods to assay function. Already several new specificities have been
found and it is clear that there are many more restriction enzyme genes in Nature
than had been previously suspected.
Autobiography on Nobel Prize website

