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

Perani, Michela, Ingram, Catherine J E, Cooper, Colin S, 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

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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
Faculty \ School: Faculty of Medicine and Health Sciences > Norwich Medical School
University of East Anglia > Faculty of Medicine and Health Sciences > Research Groups > Prostate Cancer Studies
Depositing User: Pure Connector
Date Deposited: 20 Jan 2014 16:02
Last Modified: 25 Jul 2018 09:12
URI: https://ueaeprints.uea.ac.uk/id/eprint/46166
DOI: 10.1038/sj.onc.1207031

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