Carnegie Mellon University

Monday, December 16, 2013

Luke Diorio-Toth

Luke Diorio-Toth Awarded for Best Poster Presentation

Three hundred RNA biologists from universities in the Mideast gathered for Rustbelt RNA meeting in Cleveland, Ohio on October 18-19 to discuss their latest results about the structure and function of RNA molecules. Luke Diorio-Toth, a senior chemistry major working in the Woolford laboratory, was one of six students awarded best poster presentation for his poster “Recruiting of ribosomal proteins by ribosomal assembly factors.” Luke was among 186 undergraduate and graduate presenters at the meeting.

Ribosomes, nature’s most complex ribonucleoprotein particle, catalyze protein synthesis in all cells. The Woolford lab studies how ribosomes assemble in eukaryotic cells, using the baker’s yeast, Saccharomyces cerevisiae, as a model organism. Luke and coworkers want to know how the 200 yeast ribosome assembly factors enable ribosomal RNA to fold into their proper three-dimensional structure, undergo processing to remove spacer sequences, and bind to ribosomal proteins. Luke discovered that ribosomal proteins surrounding the polypeptide exit tunnel of the large ribosomal subunit recruits the GTPase assembly factor Nog2, which then acts to strengthen the association of these ribosomal proteins with rRna. The results of Luke’s study led the Woolford lab to rethink how the GTPases reconfigure the tunnel neighborhood of the ribosome, just before nascent ribosomes are licensed for export from the nucleus to the cytoplasm.