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Mol. Cell. Biol., 08 1995, 4240-4248, Vol 15, No. 8
Copyright © 1995, American Society for Microbiology

SNF11, a new component of the yeast SNF-SWI complex that interacts with a conserved region of SNF2

I Treich, BR Cairns, T de los Santos, E Brewster and M Carlson
Institute of Cancer Research, Columbia University, New York, New York 10032, USA.

The yeast SNF-SWI complex is required for transcriptional activation of diverse genes and has been shown to alter chromatin structure. The complex has at least 10 components, including SNF2/SWI2, SNF5, SNF6, SWI1/ADR6, and SWI3, and has been widely conserved in eukaryotes. Here we report the characterization of a new component. We identified proteins that interact in the two-hybrid system with the N-terminal region of SNF2, preceding the ATPase domain. In addition to SWI3, we recovered a new 19-kDa protein, designated SNF11. Like other SNF/SWI proteins, SNF11 functions as a transcriptional activator in genetic assays. SNF11 interacts with SNF2 in vitro and copurifies with the SNF- SWI complex from yeast cells. Using a specific antibody, we showed that SNF11 coimmunoprecipitates with members of the SNF-SWI complex and that SNF11 is tightly and stoichiometrically associated with the complex. Furthermore, SNF11 was detected in purified SNF-SWI complex by staining with Coomassie blue dye; its presence previously went unrecognized because it does not stain with silver. SNF11 interacts with a 40- residue sequence of SNF2 that is highly conserved, suggesting that SNF11 homologs exist in other organisms.


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