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Perani, Michela, Ingram, Catherine J E, Cooper, Colin S 
ORCID: https://orcid.org/0000-0003-2013-8042, Garrett, Michelle D and Goodwin, Graham H
(2003)
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 (50).
pp. 8156-67.
ISSN 0950-9232
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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | amino acid sequence,animals,cos cells,chromatin,conserved sequence,humans,neurotensin,protein structure, tertiary,proteins,proto-oncogene proteins,repressor proteins,transcription factors,vasoactive intestinal peptide,sdg 3 - good health and well-being ,/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_being |
| Faculty \ School: | Faculty of Medicine and Health Sciences > Norwich Medical School |
| UEA Research Groups: | Faculty of Medicine and Health Sciences > Research Groups > Cancer Studies |
| Depositing User: | Pure Connector |
| Date Deposited: | 20 Jan 2014 16:02 |
| Last Modified: | 24 Oct 2022 05:33 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/46166 |
| DOI: | 10.1038/sj.onc.1207031 |
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