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Five SWI/SNF gene products are components of a large multisubunit complex required for transcriptional enhancement.

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  • 1. Program in Molecular Medicine, University of Massachussetts Medical Center, Worcester 01605.
      Authors
    • Peterson CL 1
    (1 author)

Proceedings of the National Academy of Sciences of the United States of America, 01 Apr 1994, 91(8):2905-2908
https://doi.org/10.1073/pnas.91.8.2905 PMID: 8159677 PMCID: PMC43482

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A comment on this article appears in "Dissecting a complex process." Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):2886-7.

Abstract 

The Saccharomyces cerevisiae SWI1, SWI2 (SNF2), SWI3, SNF5, and SNF6 gene products play a crucial role in the regulation of transcription. We provide here direct biochemical evidence that all five SWI/SNF polypeptides are components of a large multisubunit complex. These five polypeptides coelute from a gel-filtration column with an apparent molecular mass of approximately 2 MDa. The five SWI/SNF polypeptides do not copurify when extracts are prepared from swi- or snf- mutants. We show that SWI/SNF polypeptides also remain associated during an affinity-chromatography step followed by gel filtration. Assembly of the SWI/SNF complex is not disrupted by a mutation in the putative APT-binding site of SWI2, although this mutation eliminates SWI2 function.

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Proc Natl Acad Sci U S A. 1994 Apr 12; 91(8): 2905–2908.
PMCID: PMC43482
PMID: 8159677

Five SWI/SNF gene products are components of a large multisubunit complex required for transcriptional enhancement.

C L Peterson, A Dingwall, and M P Scott
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Abstract

The Saccharomyces cerevisiae SWI1, SWI2 (SNF2), SWI3, SNF5, and SNF6 gene products play a crucial role in the regulation of transcription. We provide here direct biochemical evidence that all five SWI/SNF polypeptides are components of a large multisubunit complex. These five polypeptides coelute from a gel-filtration column with an apparent molecular mass of approximately 2 MDa. The five SWI/SNF polypeptides do not copurify when extracts are prepared from swi- or snf- mutants. We show that SWI/SNF polypeptides also remain associated during an affinity-chromatography step followed by gel filtration. Assembly of the SWI/SNF complex is not disrupted by a mutation in the putative APT-binding site of SWI2, although this mutation eliminates SWI2 function.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
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