Date of Award

8-1-2015

Degree Name

Master of Science

Department

Molecular Biology Microbiology and Biochemistry

First Advisor

Bartholomew, Blaine

Second Advisor

Davie, Judy

Abstract

Combined with the data showing that the analogous section of BRG1 has histone binding properties, the second proposed model, where the SnAC domain acts as a histone anchor required for remodeling and directly binds to a location on the histone surface, was pursued. This was supported by Fe-BABE targeted cleavage that showed a cleavage site located within the SnAC domain as well as crosslinking data that showed there was a 2-3 fold reduction of Snf2 crosslinking upon deletion of the SnAC domain [62]. In order to find which histones SnAC binds to specifically and the regions of the histone(s) involved, a recombinant SnAC domain protein was generated and used in pull down assays with histones H2A, H3, and H4 in order to show binding and specificity. Finally gH3, a tailless histone H3, was purified to determine if the interaction between the SnAC domain and the histone occurred in either the tail, or core domain of the protein.

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