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

By H. Kato, A. Tjernberg, W. Zhang, A.N. Krutchinsky, W. An, T. Takeuchi, Y. Ohtsuki, S. Sugano, D.R.H. de Bruijn, B.T. Chait and R.G. Roeder

Abstract

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

Publisher: 'American Society for Biochemistry & Molecular Biology (ASBMB)'
Year: 2002
DOI identifier: 10.1074/jbc.m108702200
OAI identifier:
Provided by: NARCIS
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