Brian D. Strahl

Eukaryotic genomes are packaged into the nuclei of cells through the actions of histone proteins. These proteins not only play a role in condensing the genome but are fundamental to establishing and maintaining chromatin domains such as euchromatin and heterochromatin. Our lab is addressing how chromatin organization achieved and what factors make the underlying DNA permissive to the protein machineries that drive transcription, replication, recombination, and repair. A large body of work shows that histone post-translational modifications are central to the regulation of chromatin structure and function. These modifications, which include acetylation and methylation, decorate histones and function, at least in part, by recruiting chromatin regulatory proteins to the sites of these modifications. Current efforts are aimed at understanding how histone modifications are installed and removed, and how they are interpreted to regulate genome function.