Donald C. Rio

Biosketch

Donald Rio is a biochemist and molecular biologist who studies nucleic rearrangement reactions. His work has uncovered fundamental mechanisms of how eukaryotic mobile DNA elements or transposons, are mobilized and how their movement is regulated. Rio grew up in central Connecticut. He graduated from the University of Colorado, Boulder in 1979 with a bachelor’s degree in Chemistry and Biology and from the University of California, Berkeley in 1983 with a Ph.D. in Biochemistry. After completing his postdoctoral studies at the University of California, Berkeley, he joined the faculty of the Whitehead Institute for Biomedical Research and the Massachusetts Institute of Technology (MIT) in 1987. He moved back to the University of California, Berkeley in 1992. At Berkeley he has served as Head of the Division of Genetics, Genomics Development and as Co-Chair of the Department of Molecular and Cell Biology (MCB). He is the Goldman Distinguished Chair in the Biological Sciences and a Professor of Biochemistry, Biophysics and Structural Biology. Rio has been elected to the National Academy of Sciences.

Research Interests

The Rio laboratory studies eukaryotic transposable elements and alternative pre-messenger RNA (pre-mRNA) splicing. By combining biochemical, cell-based and genetic assays, mechanisms about how eukaryotic transposable elements move, how their mobility is controlled and how RNA binding proteins control alternative pre-mRNA splicing have been elucidated. The P transposable element from the fruit fly, Drosophila, has been the main model system and using an elegant combination of biochemical purification and reconstitution, in vivo assays and structural biology, the assembly of transposase protein-DNA complexes, the mechanism of transposition, its cofactors and DNA rearrangements were elucidated and more generally how DNA-based transposons move around animal genomes. P element mobility is normally restricted to the Drosophila germline at the post-transcriptional level by alternative pre-mRNA splicing. Rio and colleagues used a combination of biochemical purification, in vitro and genetic assays to identify and define the action of a series of RNA binding proteins and the spliceosomal U1 snRNP (small nuclear ribonucleoprotein) in the inhibition of P element transposase pre-mRNA splicing. Assembly of these components at an exonic RNA splicing silencer (ESS) element prevents production of the transposase mRNA in somatic cells. The elucidation of the mode of action of these proteins provided more general insights into how RNA binding proteins control patterns of alternative splicing.