Source:http://linkedlifedata.com/resource/pubmed/id/16648632
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
26
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pubmed:dateCreated |
2006-6-26
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pubmed:abstractText |
The SWI/SNF and SAGA chromatin-modifying complexes contain bromodomains that help anchor these complexes to acetylated promoter nucleosomes. To study the importance of bromodomains in these complexes, we have compared the chromatin-remodeling and octamer-transfer activity of the SWI/SNF complex to a mutant complex that lacks the Swi2/Snf2 bromodomain. Here we show that the SWI/SNF complex can remodel or transfer SAGA-acetylated nucleosomes more efficiently than the Swi2/Snf2 bromodomain-deleted complex. These results demonstrate that the Swi2/Snf2 bromodomain is important for the remodeling as well as for the octamer-transfer activity of the complex on H3-acetylated nucleosomes. Moreover, we show that, although the wild-type SWI/SNF complex displaces SAGA that is bound to acetylated nucleosomes, the bromodomain mutant SWI/SNF complex is less efficient in SAGA displacement. Thus, the Swi2/Snf2 bromodomain is required for the full functional activity of SWI/SNF on acetylated nucleosomes and is important for the displacement of SAGA from acetylated promoter nucleosomes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleosomes,
http://linkedlifedata.com/resource/pubmed/chemical/SAGA complex, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SNF2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18126-34
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16648632-Acetylation,
pubmed-meshheading:16648632-Adenosine Triphosphatases,
pubmed-meshheading:16648632-Chromatin,
pubmed-meshheading:16648632-DNA-Binding Proteins,
pubmed-meshheading:16648632-Gene Expression Regulation, Fungal,
pubmed-meshheading:16648632-Nucleosomes,
pubmed-meshheading:16648632-Promoter Regions, Genetic,
pubmed-meshheading:16648632-Protein Structure, Tertiary,
pubmed-meshheading:16648632-Saccharomyces cerevisiae,
pubmed-meshheading:16648632-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:16648632-Trans-Activators,
pubmed-meshheading:16648632-Transcription Factors
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pubmed:year |
2006
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pubmed:articleTitle |
The Swi2/Snf2 bromodomain is required for the displacement of SAGA and the octamer transfer of SAGA-acetylated nucleosomes.
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pubmed:affiliation |
Faculty of Medicine and Health Sciences, Department of Biochemistry, United Arab Emirates University, P. O. Box 17666, Al-Ain, United Arab Emirates. ahmedh@uaeu.ac.ae
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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