Heterochromatin in "S. cerevisiae" is composed of a wide array of proteins and plays several roles. The first stage of heterochromatin formation requires DNA binding proteins, which interact with specific cis DNA sequences at the telomeres, rDNA and HM loci. These proteins, including Rap1p and the origin recognition complex (ORC), serve as a platform for other proteins to bind, condense the DNA, and modify neighboring histones. Some of these proteins, notably Rap1p, also play other roles, including initiation of transcription. The first known step in the formation of dedicated heterochromatin is the binding of Sir4p to Rap1p (Luo, Vega-Palas et al. 2002). Sir4p is one of four ‘Silent Information Regulator’ proteins that also include Sir1p, Sir2p and Sir3p. Of these, Sir2p, Sir3p and Sir4p form the core of heterochromatin. Sir4p serves as a binding site for Sir2p, which is the next to bind. Sir2p deacetylates adjacent histones, which is thought to further condense the chromatin and prevent the binding of other transcription promoting histone modification enzymes. Sir3p binding follows, further condensing the heterochromatin. Sir1p plays a role in the initiation of silencing at the HM loci. A large number of other proteins act in both a synergistic and antagonistic manner.