Abstract
The SWI/SNF protein complex is required for the enhancement of transcription by many transcriptional activators in yeast. Here it is shown that the purified SWI/SNF complex is composed of 10 subunits and includes the SWI1, SWI2/SNF2, SWI3, SNF5, and SNF6 gene products. The complex exhibited DNA-stimulated adenosine triphosphatase (ATPase) activity, but lacked helicase activity. The SWI/SNF complex caused a 10- to 30-fold stimulation in the binding of GAL4 derivatives to nucleosomal DNA in a reaction that required adenosine triphosphate (ATP) hydrolysis but was activation domain-independent. Stimulation of GAL4 binding by the complex was abolished by a mutant SWI2 subunit, and was increased by the presence of a histone-binding protein, nucleoplasmin. A direct ATP-dependent interaction between the SWI/SNF complex and nucleosomal DNA was detected. These observations suggest that a primary role of the SWI/SNF complex is to promote activator binding to nucleosomal DNA.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 8:01 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 14, 2024, 11:07 p.m.) |
Indexed | 2 days, 2 hours ago (Aug. 20, 2025, 8:32 a.m.) |
Issued | 31 years, 1 month ago (July 1, 1994) |
Published | 31 years, 1 month ago (July 1, 1994) |
Published Print | 31 years, 1 month ago (July 1, 1994) |
@article{C_t__1994, title={Stimulation of GAL4 Derivative Binding to Nucleosomal DNA by the Yeast SWI/SNF Complex}, volume={265}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.8016655}, DOI={10.1126/science.8016655}, number={5168}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Côté, Jacques and Quinn, Janet and Workman, Jerry L. and Peterson, Craig L.}, year={1994}, month=jul, pages={53–60} }