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SYT associates with human SNF/SWI complexes and the C-terminal region of its fusion partner SSX1 targets histones.

A global transcriptional co-activator, the SNF/SWI complex, has been characterized as a chromatin remodeling factor that enhances accessibility of the transcriptional machinery to DNA within a repressive chromatin structure. On the other hand, mutations in some human SNF/SWI complex components have been linked to tumor formation. We show here that SYT, a partner protein generating the synovial sarcoma fusion protein SYT-SSX, associates with native human SNF/SWI complexes. The SYT protein has a unique QPGY domain, which is also present in the largest subunits, p250 and the newly identified homolog p250R, of the corresponding SNF/SWI complexes. The C-terminal region (amino acids 310-387) of SSX1, comprising the SSX1 portion of the SYT-SSX1 fusion protein, binds strongly to core histones and oligonucleosomes in vitro and directs nuclear localization of a green fluorescence protein fusion protein. Experiments with serial C-terminal deletion mutants of SSX1 indicate that these properties map to a common region and also correlate with the previously demonstrated anchorage-independent colony formation activity of SYT-SSX in Rat 3Y1 cells. These data suggest that SYT-SSX interferes with the function of either the SNF/SWI complexes or another SYT-interacting co-activator, p300, by changing their targeted localization or by directly inhibiting their chromatin remodeling activities.

Pubmed ID: 11734557

Authors

  • Kato H
  • Tjernberg A
  • Zhang W
  • Krutchinsky AN
  • An W
  • Takeuchi T
  • Ohtsuki Y
  • Sugano S
  • de Bruijn DR
  • Chait BT
  • Roeder RG

Journal

The Journal of biological chemistry

Publication Data

February 15, 2002

Associated Grants

  • Agency: NCI NIH HHS, Id: CA42567
  • Agency: NCRR NIH HHS, Id: RR00862

Mesh Terms

  • Amino Acid Sequence
  • Cell Line
  • Cell Nucleus
  • Chromatin
  • Electrophoresis, Polyacrylamide Gel
  • Gene Deletion
  • Glutathione Transferase
  • HeLa Cells
  • Histones
  • Humans
  • Immunoblotting
  • Models, Genetic
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Plasmids
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases
  • Proteins
  • Proto-Oncogene Proteins
  • Recombinant Fusion Proteins
  • Repressor Proteins
  • Transcription Factors
  • Transcription, Genetic