The function of YEATS domain proteins in S. cerevisiae

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In eukaryotes DNA is packaged into a nucleoprotein structure consisting of DNA, histones, and non-histone proteins. The packing of DNA into chromatin is important for the regulation of gene expression and for chromosome stability. Chromatin structure can be regulated by the addition of post-translational modifications to histones, including acetylation, methylation, phosphorylation, and ubiquitination. However, despite several decades of study, little is known regarding the functional consequences of these histone modifications. The current accepted hypothesis is that histone post-translational modifications serve as "beacons" to recruit "effector" proteins that modify chromatin structure. However, to date, few of these effector proteins have been identified. We have recently detected chromatin-binding activity in Yaf9p, a YEATS (Yaf9-ENL-AF9-Taf14-Sas5) domain-containing protein. Proteins containing YEATS domains are components of multiple chromatin modifying complexes, and we are interested in determining whether these proteins specifically recognize post-translationally modified histones. Using a combination of genetic and biochemical approaches we will characterize the interaction of the YEATS-domain proteins with chromatin in the model organism, Saccharomyces cerevisiae. Determining the function of these proteins will enable us to understand how histone modifications can regulate chromatin structure.