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Conserved SNH domain of the proto-oncoprotein SYT interacts with components of the human chromatin remodelling complexes, while the QPGY repeat domain forms homo-oligomers

Oncogene volume 22, pages 8156–8167 (2003)Cite this article

Abstract

Many studies have now established that the SWI/SNF chromatin remodelling complexes are involved in activation and repression of a variety of genes. In mammalian cells, these complexes contain the BRM and BRG1 helicase-like proteins that are thought to be responsible for nucleosome remodelling. The proto-oncoprotein SYT, involved in the unique translocation t(X;18) found in synovial sarcoma, is known to interact with human BRM (hBRM), thus providing a link between chromatin remodelling factors and human cancer. In this work, we address how SYT interacts with hBRM and BRG1. We demonstrate that the conserved N-terminal SNH domain of SYT, which is also present in the oncoproteins SYT-SSX, binds to both hBRM and BRG1. We have also found that in vivo the C-terminus transactivation QPGY region of SYT can interact with itself. This results in an amplified interaction with hBRM and highlights a possible regulatory function of this domain in cells.

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Acknowledgements

We would like to thank Nina Perusinghe for the technical assistance with confocal microscopy. This work was supported by the Cancer Research UK and the Association of International Cancer Research.

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  1. Section of Molecular Carcinogenesis – BLB, Institute of Cancer Research, 15,Cotswold Road, Sutton, SM 5NG, Surrey, UK

    Michela Perani, Catherine JE Ingram, Colin S Cooper & Graham H Goodwin

  2. Cancer Research UK Centre for Cancer Therapeutics at The Institute of Cancer Research, Sutton, Surrey, UK

    Michelle D Garrett

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  1. Michela Perani
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  2. Catherine JE Ingram
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Correspondence to Michela Perani.

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Perani, M., Ingram, C., Cooper, C. et al. Conserved SNH domain of the proto-oncoprotein SYT interacts with components of the human chromatin remodelling complexes, while the QPGY repeat domain forms homo-oligomers. Oncogene 22, 8156–8167 (2003). https://doi.org/10.1038/sj.onc.1207031

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