The objective of this research is to identify and initiate functional characterization of the SWI/SNF complex in the unique chromatin environment of Tetrahymena thermophila. Through affinity purification followed by mass spectrometry (AP-MS), we identified the first SWI/SNF complex in protists through the reciprocal interaction of Snf5 and a small bromodomain containing protein (Ibd1). Through AP-MS of Ibd1 I found Ibd1 is versatile and interacts with several additional putative chromatin remodeling complexes such as a HMT, and SAGA and SWR. Bromodomains have affinity for acetylated lysine residues. Our peptide array experiment suggests that Ibd1 has affinity to multiple acetylated PTM related to highly transcribed regions. We found that indirect immunofluorescence (IF) of Ibd1 hints at a role in transcription. We are developing a protocol to use ChIP-Seq to identify the Ibd1 binding sites in the genome during growth.