Use of DNA photoaffinity labeling to study nucleosome remodeling by SWI/SNF

Sarojini M. Sengupta; Jim Persinger; Blaine Bartholomew; Craig L. Peterson

doi:10.1006/meth.1999.0880

Use of DNA photoaffinity labeling to study nucleosome remodeling by SWI/SNF

Sarojini M. Sengupta, Jim Persinger, Blaine Bartholomew, Craig L. Peterson

Research output: Contribution to journal › Article › peer-review

19 Scopus citations

Abstract

The ability of large protein assemblies to reorganize chromatin in an ATP-dependent manner is an important process for regulation of gene expression and potentially for DNA replication and recombination. The manner in which these proteins remodel chromatin to make the DNA accessible to DNA binding proteins such as transcription factors is not well understood. Site-directed DNA-protein cross-linking has been used to understand the architecture of the SWI/SNF-nucleosomal complex and the mechanistic details of how the nucleosome is remodeled. A detailed protocol for such a study is presented along with examples of the extent of this approach.

Original language	English (US)
Pages (from-to)	434-446
Number of pages	13
Journal	Methods: A Companion to Methods in Enzymology
Volume	19
Issue number	3
DOIs	https://doi.org/10.1006/meth.1999.0880
State	Published - Nov 1999
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
General Biochemistry, Genetics and Molecular Biology

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10.1006/meth.1999.0880

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abstract = "The ability of large protein assemblies to reorganize chromatin in an ATP-dependent manner is an important process for regulation of gene expression and potentially for DNA replication and recombination. The manner in which these proteins remodel chromatin to make the DNA accessible to DNA binding proteins such as transcription factors is not well understood. Site-directed DNA-protein cross-linking has been used to understand the architecture of the SWI/SNF-nucleosomal complex and the mechanistic details of how the nucleosome is remodeled. A detailed protocol for such a study is presented along with examples of the extent of this approach.",

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AB - The ability of large protein assemblies to reorganize chromatin in an ATP-dependent manner is an important process for regulation of gene expression and potentially for DNA replication and recombination. The manner in which these proteins remodel chromatin to make the DNA accessible to DNA binding proteins such as transcription factors is not well understood. Site-directed DNA-protein cross-linking has been used to understand the architecture of the SWI/SNF-nucleosomal complex and the mechanistic details of how the nucleosome is remodeled. A detailed protocol for such a study is presented along with examples of the extent of this approach.

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Use of DNA photoaffinity labeling to study nucleosome remodeling by SWI/SNF

Abstract

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