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.
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.
Mesh Terms:
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
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
Oncogene
Date: Nov. 06, 2003
PubMed ID: 14603256
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