We are interested elucidating the mechanisms by which the core histone tail domains define the structural and functional state of nucleosomes and the chromatin fiber. To this end we prepare well-defined model chromatin complexes and chemically and spectroscopically probe structure and interactions in solution.
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We are investigating how chromatin structure effects the activity of DNA-modifying enzymes involved in DNA replication and base-excision repair (BER). Specifically, we have found that two enzymes involved in these processes, human DNA ligase I and FEN1, are able to operate surprisingly efficiently on nucleosome substrates.
Learn more about Chromatin Structure Affects the Activity of DNA-Modifying Enzymes
We have been investigating the mechanisms by which chromatin remodeling complexes use the energy of ATP hydrolysis to alter structure and accessibility in nucleosomes. Working with our collaborators has allowed us to investigate several aspects of the hSWI/SNF complex.
Learn more about Mechanisms of ATP-dependent Chromatin Remodeling Complexes