Proceedings of the National Academy of Sciences of the United States of America

About the PNAS Member Editor
Name Bass, Brenda L.
Location University of Utah
Primary Field Biochemistry
 Election Citation
Bass pioneered understanding of the biological functions of double-stranded (ds)RNA and of the proteins mediating these roles. She discovered the unwinding enzyme ADAR and elucidated its mechanism, enabling prediction of editing sites in dsRNA. Her studies of the RNA interference enzyme Dicer have established links between dsRNA and cellular stress.
 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.

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