Literature DB >> 20513433

SWI/SNF has intrinsic nucleosome disassembly activity that is dependent on adjacent nucleosomes.

Mekonnen Lemma Dechassa1, Abdellah Sabri, Santhi Pondugula, Stefan R Kassabov, Nilanjana Chatterjee, Michael P Kladde, Blaine Bartholomew.   

Abstract

The ATP-dependent chromatin remodeling complex SWI/SNF regulates transcription and has been implicated in promoter nucleosome eviction. Efficient nucleosome disassembly by SWI/SNF alone in biochemical assays, however, has not been directly observed. Employing a model system of dinucleosomes rather than mononucleosomes, we demonstrate that remodeling leads to ordered and efficient disassembly of one of the two nucleosomes. An H2A/H2B dimer is first rapidly displaced, and then, in a slower reaction, an entire histone octamer is lost. Nucleosome disassembly by SWI/SNF did not require additional factors such as chaperones or acceptors of histones. Observations in single molecules as well as bulk measurement suggest that a key intermediate in this process is one in which a nucleosome is moved toward the adjacent nucleosome. SWI/SNF recruited by the transcriptional activator Gal4-VP16 preferentially mobilizes the proximal nucleosome and destabilizes the adjacent nucleosome. Copyright 2010 Elsevier Inc. All rights reserved.

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Year:  2010        PMID: 20513433      PMCID: PMC3161732          DOI: 10.1016/j.molcel.2010.02.040

Source DB:  PubMed          Journal:  Mol Cell        ISSN: 1097-2765            Impact factor:   17.970


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