School of Life Sciences, University of Dundee, Dundee, UK
Visiting professor Xiamen University, Nankai University and the University of the Chinese Academy of Sciences.
Professor Lilley has a long-standing interest in nucleic acid structure and function (both DNA and RNA) going back more than forty years.
He was the first to solve the structure of the Holliday junction in DNA, and has made extensive studies of its interaction with junction-resolving enzymes. He has solved the crystal structure of a complex with eukaryotic GEN1 resolving enzyme.
Lilley has had a long interest in the structures and mechanisms of RNA catalysis. He has solved crystal structures of the twister, TS and pistol ribozymes, and defined their chemical mechanisms. Most recently he has determined the structure of a methyltransferase ribozyme, and shown that it employs a remarkably sophisticated catalytic mechanism that involves nucleobase-mediated general acid catalysis. His lab has solved crystal structures of seven different riboswitches, the most recent being a new NAD+ riboswitch.
Lilley has made a detailed study of the structure and folding of the k-turn motif. This is arguably now the best understood structural motif in RNA. Recently he has shown how N6-methylation of a critical adenine blocks the key first stages of box C/D snoRNP assembly.
Professor Lilley is an elected fellow of the Royal Society.