Literature DB >> 32917506

Nucleosomes Meet Their Remodeler Match.

Jonathan Markert1, Karolin Luger2.   

Abstract

Over 85% of all genomic DNA in eukaryotes is organized in arrays of nucleosomes, the basic organizational principle of chromatin. The tight interaction of DNA with histones represents a significant barrier for all DNA-dependent machineries. This is in part overcome by enzymes, termed ATP-dependent remodelers, that are recruited to nucleosomes at defined locations and modulate their structure. There are several different classes of remodelers, and all use specific nucleosome features to bind to and alter nucleosomes. This review highlights and summarizes areas of interactions with the nucleosome that allow remodeling to occur.
Copyright © 2020 Elsevier Ltd. All rights reserved.

Keywords:  ATP-dependent chromatin-remodeling factor; DNA accessibility; cryo-EM; nucleosome

Mesh:

Substances:

Year:  2020        PMID: 32917506     DOI: 10.1016/j.tibs.2020.08.010

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  6 in total

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4.  SMARCAD1 is an ATP-dependent histone octamer exchange factor with de novo nucleosome assembly activity.

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Review 5.  The Mediator complex as a master regulator of transcription by RNA polymerase II.

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  6 in total

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