BIOL 65 |
| It has been postulated that covalent post-translational modifications of histones comprise a code that may selectively interact with chromatin-associated components. Bromodomains (BDs) may play a key role in initiating site-specific assembly events by binding acetyl-lysines on histone proteins. To study the BDhistone interactions and understand the acetylation dependence of binding, the Polybromo-1 subunit of Polybromo, BRG1 associated factors (PBAF) chromatin remodeling complex was chosen. The protein contains six tandem BDs and provides a unique model system to understand the initial binding events. Fluorescence anisotropy was used to screen and quantify the interaction between individual bromodomains and acetylated peptides containing the histone H3 tail sequence. To better understand the site-specific binding events, rigorous thermodynamic analyses were also performed. Individual BDs show significant variation in the salt and temperature dependence of histone binding. Ultimately, analysis of BD-histone interactions can be used to develop hypotheses regarding the histone acetylation pattern(s) targeted by PBAF. |
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Protein Structure and Folding
4:30 PM-6:30 PM, Sunday, 10 September 2006 Moscone Center -- Hall D, Poster
Division of Biological Chemistry |