Brenda L. Bass
University of Utah
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Primary Section: 21, Biochemistry Membership Type:
Member
(elected 2015)
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Biosketch
Brenda Bass is a Distinguished Professor in the Department of Biochemistry at the University of Utah School of Medicine. She is known for her contributions in defining double-stranded RNA-mediated pathways, including those involving the ADAR RNA editing enzymes, and Dicer, a key enzyme in RNA interference. Bass was born in Fort Lauderdale, Florida, in 1955. She graduated from Colorado College, Colorado Springs, Colorado, in 1977 with a BA in chemistry, and from the University of Colorado, Boulder, in 1985 with a PhD in chemistry. She was a postdoctoral fellow at the Fred Hutchinson Cancer Research Center prior to joining the faculty of the University of Utah School of Medicine in 1989. She served as president of the RNA Society in 2007 and is also a member of the American Academy of Arts and Sciences and a fellow of the American Association for the Advancement of Science.
Research Interests
Research in the Bass laboratory is focused on understanding the biological functions of long double-stranded RNA (dsRNA) and dsRNA binding proteins (dsRBPs). Viruses were once thought to be the sole source of long dsRNA, but the Bass laboratory has identified numerous long dsRNAs that naturally exist in animals, primarily focusing on C. elegans and mammals. Proteins that recognize dsRNA are not sequence-specific, and the Bass laboratory is interested in how these proteins distinguish endogenous and viral dsRNA, as well as how endogenous dsRNA-mediated pathways coexist. Their studies indicate dsRNA-mediated pathways intersect and compete for dsRNA substrates. For example, altered levels of the dsRBP ADAR, an RNA editing enzyme, or altered levels of dsRNA, alters the levels of the small RNAs produced by the dsRBP Dicer. In addition to molecular biology, bioinformatics, and in vivo studies in C. elegans and mammalian cells, the Bass laboratory relies on biochemistry studies for insight. Biochemical studies of Dicer revealed that the ends, or termini, of dsRNA are important for its recognition, possibly providing a way to distinguish viral and cellular dsRNA. Biochemical and structural studies of ADAR revealed inositol hexakisphosphate as an essential cofactor.
