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The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle

Nature Structural & Molecular Biology volume 20, pages 1119–1121 (2013)Cite this article

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Abstract

The N-terminal acetylation of Sir3 is essential for heterochromatin establishment and maintenance in yeast, but its mechanism of action is unknown. The crystal structure of the N-terminally acetylated BAH domain of Saccharomyces cerevisiae Sir3 bound to the nucleosome core particle reveals that the N-terminal acetylation stabilizes the interaction of Sir3 with the nucleosome. Additionally, we present a new method for the production of protein–nucleosome complexes for structural analysis.

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Figure 1: Sir3 N-terminal acetylation increases Sir3 BAH affinity for NCPs.
Figure 2: Sir3 N-terminal acetylation stabilizes the interaction of Sir3 BAH with the NCP.

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Acknowledgements

We thank G. Murshudov, F. Long, R. Nicholls, P. Emsley and H. Powell for troubleshooting and sharing tools for the software Refmac5, LibG, Prosmart, Coot and iMosflm. We thank M. Lamers and K. Nagai's laboratory for critical discussion of the results. We thank M. Yu for helping with the usage of the I24 beamlines at Diamond Light Source. F.M. is supported by the Swiss National Fund (PBGEP3-123695), a European Molecular Biology Organization Long Term Fellowship (ALTF419-2009) and a Marie Curie Intra European Long Term Fellowship (FP7-PEOPLE-2009-IEF-251794). N.A. is supported by the EU FP7 Marie Curie Initial training Nucleosome 4D network (4609511-238176). The project was supported by the UK Medical Research Council (MC-A025-5PJ80).

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  1. Daniela Rhodes

    Present address: Present address: School of Biological Sciences, Nanyang Technological University, Singapore.,

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  1. Structural Studies Division, Medical Research Council–Laboratory of Molecular Biology, Cambridge, UK

    Nadia Arnaudo, Israel S Fernández, Stephen H McLaughlin, Sew Y Peak-Chew, Daniela Rhodes & Fabrizio Martino

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  1. Nadia Arnaudo
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  2. Israel S Fernández
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  3. Stephen H McLaughlin
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Contributions

D.R., F.M. and N.A. designed the experiments. F.M. and N.A. purified all the proteins, DNA and complexes used, prepared, optimized and cryoprotected the crystals, solved the structure and wrote the manuscript. I.S.F. froze the crystals. F.M., N.A. and I.S.F. collected the X-ray diffraction data. N.A. and S.H.M. performed the binding experiments. S.Y.P.-C. performed the MALDI. D.R. revised the manuscript.

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Correspondence to Fabrizio Martino.

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The authors declare no competing financial interests.

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Supplementary Figures 1–3 and Supplementary Table 1 (PDF 4433 kb)

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Arnaudo, N., Fernández, I., McLaughlin, S. et al. The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle. Nat Struct Mol Biol 20, 1119–1121 (2013). https://doi.org/10.1038/nsmb.2641

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