Abstract
Post-translational modifications (PTMs) on histone tails are important for many DNA-templated processes, including transcription elongation by RNA polymerase II (RNAPII). Histone PTMs directly alter the accessibility of chromatin and serve as binding sites for effector proteins that mediate numerous downstream biological processes. During transcription elongation in budding yeast (Saccharomyces cerevisiae), the C-terminal domain of RNAPII is hyperphosphorylated at serines 2 and 5 (Ser2 and Ser5) of the YSPTSPS consensus repeat. The histone methyltransferase (HMT) Set2 is recruited to phosphorylated Ser2 and Ser5, promoting the catalysis of lysine 36 (H3K36) methylation on the nucleosomal H3 tail in the bodies of genes. H3K36 methylation is recognized by the Rpd3S histone deacetylase (HDAC) complex, consisting of Rpd3, Sin3, Ume1, Rco1, and Eaf3. Deacetylation of histones behind elongating RNAPII has been shown to suppress cryptic initiation of transcription within the bodies of genes by decreasing chromatin accessibility. While it has been shown that recognition of H3K36 methylation by Rpd3S requires both the chromodomain of Eaf3 and the first PHD domain (PHD1) of Rco1, little is known regarding the importance of other potential histone-interacting domains within the complex. We are specifically interested in the second PHD domain (PHD2) of Rco1 due to its sequence homology to PHD1. We hypothesize that the second PHD domain of Rco1 contributes to the recognition of the Rpd3S complex on nucleosomes. Using a combination of yeast genetics and in vitro biochemical and biophysical assays, we are gaining a better understanding of the functional role of Rco1 PHD2. This study will lend insight into the importance of recognition of histone modifications by multi-domain protein complexes, and will allow us to better understand the function of the Rpd3S complex.
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