Illuminating the biochemistry of zinc and RNA in live cells

Seminar | January 27 | 4-5 p.m. | 106 Stanley Hall

 Amy Palmer, University of Colorado Boulder

 College of Chemistry

There are over two thousand proteins encoded by the human genome that are predicted to bind zinc, where zinc binding is predicted to be essential for function. At the cellular level zinc is important for DNA synthesis, cell proliferation, differentiation, and apoptosis. Given the importance of Zn2+ in cell biology and human health, it is astounding that we still don’t understand the mechanisms of how Zn2+ levels and dynamics impact basic cellular functions and give rise to disease. Although the conventional view of Zn2+ in biology is that it is constitutively and stably bound to the proteins that comprise the zinc proteome, there is growing evidence that the proteome may sense and respond to Zn2+ dynamics in cells. This talk will focus on our discoveries that Zn2+ dynamics profoundly influence fundamental cellular processes such as gene expression, interactions between transcription factors and chromatin at the single molecule level, secretory pathway function, and the proliferation-quiescence decision in the mammalian cell cycle. I will also briefly touch upon our ongoing efforts to develop Riboglow. Recently, my lab exploited our expertise in tool development, biophysical and photophysical characterization of fluorescent probes, and analytical approaches to live cell measurements, to develop a new platform for tagging mRNA and ncRNA with fluorophores to track them in live cells. This highly modular ‘Riboglow’ platform leverages different color fluorescent dyes, linkers and riboswitch RNA tags to elicit fluorescent turn-on upon binding RNA.