The Feigon laboratory has determined the structure of a key protein-RNA complex in telomerase, an enzyme that maintains the DNA at the ends of chromosomes. Telomerase activity is important in both aging and most cancers. Using a combination of X-ray crystallography and NMR spectroscopy they determined the structure of Tetrahymena thermophila telomerase holoenzyme protein, p65, in complex with telomerase RNA, providing insights into the assembly of telomerase catalytic core. The work has been published in Molecular Cell. The work also sheds light into the ‘La-motif’ proteins, which are involved in the biogenesis of diverse RNAs in the human cells. See UCLA Newsroom article.
