In Schizosaccharomyces pombe the Snf2/HDAC containing repressor complex (SHREC) is one of the key players of transcriptional gene silencing. It harbours two different enzymatic entities – a chromatin remodeler Mit1 and a histone deacetylase Clr3. Both are linked by the scaffolding protein Clr1. Other core components are Clr2 and Chp2. To better understand the incorporation of two enzymatic functions in one complex we decided to solve x-ray structures of several SHREC components – Clr3, Mit1-Clr1 and Clr2-Clr1. We could show that the Arb2 homology domain of Clr3 is involved in binding to Clr1 and observed changes in the active site allowed us to conclude that proper folding is induced by inhibitor binding. In addition, we demonstrated that Mit1 is associating with the N-terminus of Clr1 and solved the crystal structure of the minimal interaction motif. A highly positively charged surface allows for the binding to DNA with nanomolar affinity.