Histone Deacetylases (HDACs) are enzymes that modulate chromatin structure, mediate transcriptional repression and contribute to DNA damage repair. HDAC inhibitor compounds show promise as chemotherapeutic cancer treatments through disruption of chromatin structure and interference with cancer cell replication mechanisms. HDACs are divided into four classes according to function, location and expression patterns. Class I HDACs include HDACs 1, 2 and 3, and are recruited to DNA replication sites through chromatin-associated proteins. HDACs 1 and 2 are recruited to DNA via the Chromatin Associated Factor 1 (CAF-1) complex, but the recruitment mechanism of HDAC3 is not well understood. Co-immunoprecipitation experiments found that unlike HDACs 1 and 2, HDAC3 is not associated with CAF-1. Instead, HDAC3 interacts with RbAp48 and msin3a, transcriptional corepressor proteins. Previous research has confirmed the role of HDACs in DNA damage repair. Inhibition of HDAC function induces chromatin defects, indicating disrupted DNA repair pathways. Immunofluorescent analysis in HDAC-inhibited and control cells was performed to examine the role of HDACs in damage repair. Cells with inhibited HDAC activity displayed a significant increase in gamma-H2AX foci, an indicator of double-strand breaks. When DNA damage was induced, HDAC-inhibited cells also exhibited increased CAF-1 foci, indicators of the CAF-1 protein complex. A more thorough understanding of both HDAC recruitment mechanisms and role in DNA damage repair could lead to better, more targeted cancer chemotherapies.