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The SAM domain of polyhomeotic forms a helical polymer

Nature Structural Biology volume 9, pages 453–457 (2002)Cite this article

Abstract

The polycomb group (PcG) proteins are important in the maintenance of stable repression patterns during development. Several PcG members contain a protein–protein interaction module called a SAM domain (also known as SPM, PNT and HLH). Here we report the high-resolution structure of the SAM domain of polyhomeotic (Ph). Ph-SAM forms a helical polymer structure, providing a likely mechanism for the extension of PcG complexes. The structure of the polymer resembles that formed by the SAM domain of another transcriptional repressor, TEL. The formation of these polymer structures by SAM domains in two divergent repressors suggests a conserved mode of repression involving a higher order chromatin structure.

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Figure 1
Figure 2: Polymeric structure of Ph-SAM L51R.
Figure 3: Ph-SAM self-association.
Figure 4: Comparison of Ph-SAM and TEL-SAM.

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Acknowledgements

The authors would like to thank F. Laski for providing the Drosophila cDNA library, M. Sawaya and D. Cascio for help with synchrotron data collection and A. Chamberlain, H. Tran, M. Baron, R. Ramachander and F. Qiao for helpful comments on the manuscript. J.U.B. is a Leukemia and Lymphoma Society Scholar. This work was supported by an NIHgrant.

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  1. Department of Chemistry and Biochemistry, Laboratory of Structural Biology and Molecular Medicine, Molecular Biology Institute, UCLA, 611 Charles E. Young Drive East, Los Angeles, 90095-1570, California, USA

    Chongwoo A. Kim, Mari Gingery, Rosemarie M. Pilpa & James U. Bowie

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  1. Chongwoo A. Kim
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  2. Mari Gingery
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Correspondence to James U. Bowie.

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Kim, C., Gingery, M., Pilpa, R. et al. The SAM domain of polyhomeotic forms a helical polymer. Nat Struct Mol Biol 9, 453–457 (2002). https://doi.org/10.1038/nsb802

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