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Mol Cell Biol, July 1998, p. 4157-4164, Vol. 18, No. 7
Department of Microbiology and
Immunology1 and
Department of
Biochemistry and Biophysics,2 University of
California, San Francisco, California 94143-0414
Received 19 December 1997/Returned for modification 20 January
1998/Accepted 9 April 1998
In the yeast Saccharomyces cerevisiae, the SWI-SNF
complex has been proposed to antagonize the repressive effects of
chromatin by disrupting nucleosomes. The SIN genes were
identified as suppressors of defects in the SWI-SNF complex, and the
SIN1 gene encodes an HMG1-like protein that has been
proposed to be a component of chromatin. Specific mutations
(sin mutations) in both histone H3 and H4 genes produce the
same phenotypic effects as do mutations in the SIN1 gene.
In this study, we demonstrate that Sin1 and the H3 and H4 histones
interact genetically and that the C terminus of Sin1 physically
associates with components of the SWI-SNF complex. In addition, we
demonstrate that this interaction is blocked in the full-length Sin1
protein by the N-terminal half of the protein. Based on these and
additional results, we propose that Sin1 acts as a regulatable bridge
between the SWI-SNF complex and the nucleosome.
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
The C-Terminal Domain of Sin1 Interacts with
the SWI-SNF Complex in Yeast
*
Corresponding author. Mailing address: Department of
Microbiology and Immunology, 513 Parnassus, Room HSE401, Box 0414, University of California, San Francisco, San Francisco, CA 94143-0414. Phone: (415) 476-8783. Fax: (415) 476-0939. E-mail:
ajohnson{at}socrates.ucsf.edu.
Mol Cell Biol, July 1998, p. 4157-4164, Vol. 18, No. 7
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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