Transcriptional co-activator activity of SYT is negatively regulated by BRM and Brg1

Genes Cells. 2004 May;9(5):419-28. doi: 10.1111/j.1356-9597.2004.00737.x.

Abstract

The t(X;18)(p11.2;q11.2) translocation found in synovial sarcomas results in the fusion of the SYT gene on chromosome 18 to the SSX gene on chromosome X. Although the SYT-SSX fusion proteins may trigger synovial sarcoma development, the biological functions of SYT, SSX and SYT-SSX genes are unclear. Transfections of Gal4 DNA binding domain fusion protein constructs demonstrate that SYT protein acts as a transcriptional co-activator at the C-terminal domain and that the activity is repressed through the N-terminus. The N-terminal 70 amino acids of SYT bind not only to BRM, but also to Brg1, both of which are subunits of SWI/SNF chromatin remodelling complexes. Here, we have investigated the functions of BRM and Brg1 on the repression of SYT activity. The negative regulation of SYT transcriptional co-activator activity is dependent on the ATP-hydrolysis of BRM and Brg1 in the protein complexes. This indicates that the SWI/SNF protein complexes regulate SYT activity using the chromatin remodelling activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Cell Line
  • Chromatin Assembly and Disassembly
  • Chromosomal Proteins, Non-Histone / physiology
  • DNA Helicases
  • Humans
  • Hydrolysis
  • Nuclear Proteins / physiology*
  • Proto-Oncogene Proteins / genetics
  • Proto-Oncogene Proteins / physiology*
  • Repressor Proteins / genetics
  • Repressor Proteins / physiology*
  • Transcription Factors / physiology*
  • Transcriptional Activation*

Substances

  • Chromosomal Proteins, Non-Histone
  • Nuclear Proteins
  • Proto-Oncogene Proteins
  • Repressor Proteins
  • SMARCA2 protein, human
  • SS18 protein, human
  • SWI-SNF-B chromatin-remodeling complex
  • Transcription Factors
  • Adenosine Triphosphate
  • SMARCA4 protein, human
  • DNA Helicases