BBMB Research Seminars

September 26, 2007
Jeff Hayes
Associate Professor
Johns Hopkins University
"Structure of the protein-DNA interactions within chromatin"
1414 Molecular Biology Buidling
4:10 p.m.

Despite their role in regulating chromatin structure and function at several levels, the structures and interactions of the core histone tail domains remain poorly understood. Moreover, posttranslational modifications such as acetylation of specific lysines within the tails play a critical role in regulating chromatin-based activities likely in part by directly affecting tail structures and interactions. To address these issues we have developed several chemical methods to quantitatively determine binding affinities of specific regions within individual tail domains in model chromatin complexes and to identify inter-nucleosome and inter-array interactions of these domains. Our results indicate that the tails participate in specific, conformation-dependent interactions and that acetylation does not cause a global weakening of tail binding as has been assumed but leads to a much more subtle and specific alteration in tail interactions.