C. David Allis

Chromatin, packaged by histone proteins, is the physiological template of our genomes. As such, mechanisms exist to remodel the chromatin fiber to facilitate (or repress) gene expression. His study of histone modifications led to the discovery of a key acetyltransferase in Tetrahymena which was homologous with a well-known gene coactivator in yeast, Gcn5p, which he then showed was also a acetyltransferase. His work demonstrated that acetylation is a major mechanism for gene activation in cells. His later work was directed at the study of other histone modifications such as histone phosphorylation and histone methylation. His lab proposed that a 'histone code' may exist that extends the information content of our genetic code.