BIOCHEMISTRY

Model of the yeast Sen1-dependent termination complex scanning a nascent RNA polymerase II (Pol II) transcript. Binding of terminator elements in the transcript to Nrd1 and Nab3 elicits termination of transcription in a manner dependent on the helicase activity of Sen1 and glutamate 108 of the Rpb11 subunit. From the Dave Brow lab

Cytoplasmic particles formed by the human Bicaudal-C translational repressor protein

Protein curvature in a common architecture determines the specificity of RNA-protein interactions. Biochemical, genetic and structural analyses of multiple PUF proteins bound to their RNA targets reveals that the curvature of the proteins is critical in determining which RNAs each protein binds. Wickens and T. Hall labs

Human cardiomyocyte derived from IPS cells. From the Mike Sheets lab

RNA-protein interactions inside a cell identified by “RNA tagging” A chimeric protein consisting of an RNA-binding protein (RBP) fused to a U-adding enzyme (PUP) is expressed in a cell. Binding of that RBP-PUP protein to an mRNA via a binding element (blue rectangle) marks that RNA with U’s. From the Marv Wickens lab

New families of nucleotidyl transferase enzymes. The enzyme GLD-2 was discovered in C. elegans through a combination of genetics and biochemistry (collaboration of Kimble and Wickens labs). This led to tethered function assays that revealed families of regulatory enzymes that add A’s (PAPs) or U’s (PUPs) to a wide range of RNAs. Both families have widespread roles in biology, including development, the nervous system, and disease. From the Wickens lab

U1 snRNP (red) and branchpoint bridging protein (green) binding events on 30 single molecules of pre-mRNA, seen by Colocalization Single Molecule Spectroscopy. Spliceosome E complex formation is noted by the blue bars. From the Aaron Hoskins lab

Evolutionary rewiring of RNA-protein networks. Direct biochemical analyses of RNA-protein interactions in two highly diverged fungal species demonstrates that a biological function controlled by Puf3p in one species is controlled by a different protein, Puf5p, in the other. Collaboration between the Wickens and Gasch labs

The Hoskins Lab studies how the spliceosome protein SF3b1 recognizes the RNA duplex formed between the intronic branch site and the U2 snRNA

Structure of 5’ UMP bound in the active site of Usb1. From the Sam Butcher lab