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Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain

Abstract

In Saccharomyces cerevisiae, acetylation of the Sir3 N terminus is important for transcriptional silencing. This covalent modification promotes the binding of the Sir3 BAH domain to the nucleosome, but a mechanistic understanding of this phenomenon is lacking. By X-ray crystallography, we show here that the acetylated N terminus of Sir3 does not interact with the nucleosome directly. Instead, it stabilizes a nucleosome-binding loop in the BAH domain.

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Figure 1: Structure of the Sir3 BAH domain in complex with NCP.
Figure 2: Intra- and intermolecular interactions of the acetylated N terminus and loop 1 of the Sir3 BAH domain.
Figure 3: Acetylation of Ala2 stabilizes the conformation of the NCP-binding loop 3.

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Acknowledgements

We thank Shanghai Synchrotron Radiation Facility beamline scientists for technical support during data collection and F. Yang and staff scientists at the protein science core facility at the Institute of Biophysics for help with MS analyses. This work was supported by grants from the Chinese Ministry of Science and Technology (2009CB825501 to R.-M.X.) and the Natural Science Foundation of China (90919029, 3098801 and 31210103914 to R.-M.X.).

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D.Y. and Q.F. designed and performed experiments, analyzed data and wrote the paper. M.W. carried out structure determination, analyzed data and wrote the paper. R.R., H.W., M.H. and Y.S. participated in the experiments. N.Y. and R.-M.X. designed experiments, analyzed data and wrote the paper.

Corresponding authors

Correspondence to Na Yang or Rui-Ming Xu.

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The authors declare no competing financial interests.

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Supplementary Figures 1–6 and Supplementary Table 1 (PDF 8405 kb)

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Yang, D., Fang, Q., Wang, M. et al. Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain. Nat Struct Mol Biol 20, 1116–1118 (2013). https://doi.org/10.1038/nsmb.2637

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