Sir Richard Roberts was awarded the 1993 Nobel Prize in Physiology or Medicine for the discovery of introns in eukaryotic (higher organism) DNA and the mechanism of gene splicing. His work, along with that of Phillip A. Sharp, changed our basic understanding of the structure of a gene from a continuous segment within the very long double-stranded DNA molecules to a gene that could be discontinuous.
In other words, a given gene could be present in the genetic material as several, separate segments of DNA (exons) offset by non-coding segments of DNA (introns).
The discovery of discontinuous or “split” genes was a radical departure from the previous understanding, with significant consequences for studying the flow of genetic information from DNA to protein: These split genes suggest that organisms speed up evolution by rearranging gene segments into new units. How it works is that the first RNA product synthesized from DNA contains exons and introns; it’s then “copyedited” to cut out the unnecessary introns before being expressed as a protein. Since different exons end up in the edited RNA, the same DNA region can determine the structure of a variety of proteins, a process known as alternative splicing.
“The signiﬁcance stems from the fact that it completely changed our view of what constituted a gene in eukaryotes,” Roberts said in an interview on the website of New England Biolabs, where he serves as chief scientific officer. “It had repercussions throughout eukaryotic biology and was of crucial importance for interpreting the human genome sequence, for example. It meant that all higher organisms had an extra degree of complexity in the way in which they used the information encoded in their DNA. Even today we are still learning more about how split genes are processed and ﬁnding additional complexities in the regulation of the information present in these split genes.”
Roberts serves as chief scientific officer at New England Biolabs, where his research focuses on enzyme discovery using bioinformatics. At NEB, he is also responsible for REBASE (Restriction Enzyme dataBASE), a database of all the restriction modification enzyme systems and the genes that encode them.