Structure and Function of the Saccharomyces cerevisiae Sir3 BAH Domain

• DOI: 10.1128/mcb.26.8.3256-3265.2006
• Publication Date: 2006-03-31T01:46:06Z
• Authors: Jessica J. Connelly; Peihua Yuan; Hao-Chi Hsu; Zhizhong Li; Rui-Ming Xu; Rolf Sternglanz
• Keywords: Superhelix

Previous work has shown that the N terminus of Saccharomyces cerevisiae Sir3 protein is crucial for function in transcriptional silencing. Here, we show overexpression N-terminal fragments strains lacking full-length can lead to some silencing HML and HMR. contains a BAH (bromo-adjacent homology) domain at its terminus. Overexpression this alone as long Sir1 overexpressed Sir2 Sir4 are present. closely related Orc1 also silence absence any protein. A previously characterized hypermorphic sir3 mutation, D205N, greatly improves by allows it bind DNA oligonucleosomes vitro. uncharacterized region required both domains. The structure been determined. In crystal, molecule multimerizes form left-handed superhelix. This superhelix may be relevant