RNA-binding proteins (RBPs) influence, among other things, the stability, splicing, nuclear export, and translation of their target transcripts. Identifying RBP-RNA interactions is thus of great value for understanding gene expression, cellular functions, and more.
A common method for identifying RBP targets is to cross-link and immunoprecipitate the RBP-RNA complexes from cell extracts. However, says Roy Parker of the University of Colorado Boulder, a persistent problem “is how to do this on [small] specialized subsets of cells.” After all, explains Michael Rosbash of Brandeis University in Massachusetts, “one can simply not do biochemistry on tiny amounts of material.”
Rosbash and his team have thus come up with what he calls “a geneticist’s work-around.” In his team’s approach, called Targets of RNA-binding proteins Identified By Editing (TRIBE), RBPs are fused to the catalytic domain of an RNA-editing enzyme from fruit flies. The enzyme converts adenosine nucleotides into inosines, which appear as guanosines ...
