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Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein [Mnase-seq]

ABSTRACT: We propose an interacting barrier mechanism for cooperation between Isw2-related proteins and sequence-specific DNA binding factors.

ORGANISM(S): Saccharomyces cerevisiae

PROVIDER: GSE150200 | GEO | 2020/08/31

REPOSITORIES: GEO

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Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein [RNA-Seq]

Project description:We propose an interacting barrier mechanism for cooperation between Isw2-related proteins and sequence-specific DNA binding factors.

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Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein

Project description:This SuperSeries is composed of the SubSeries listed below.

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Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein [Mnase-seq]

Project description:Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein [Mnase-seq]

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Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein

Project description:Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein

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Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein [ChIP-Seq]

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Project description:Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein [RNA-Seq]

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MNase titration-Seq of Saccharomyces cerevisiae.

Project description:We report change in the nucleosome occupancy and accessibility upon deletion of ATP-dependent chromatin remodellers (ISW1, ISW2 & CHD1) in Saccharomyces cerevisiae.

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Histone octamer structure is altered early in ISW2 ATP-dependent remodeling of nucleosomes

Project description:Histone octamers are thought to be a rigid part of nucleosomes that shape chromatin and block cellular machinery from accessing DNA. ATP-dependent chromatin remodelers like ISW2 mobilize nucleosomes to provide DNA access. We find evidence for histone octamer distortion preceding DNA being moved into nucleosomes and processive movement of the ATPase motor of ISW2 on nucleosomal DNA. DNA entering nucleosome is uncoupled from the ATPase activity of ISW2 and alterations of the histone octamer structure mediated by ISW2 by deletion of the SANT domain from the C-terminus of the Isw2 catalytic subunit. We also find that restricting histone movement by chemical crosslinking traps remodeling intermediates resembling those seen by loss of the SANT domain, further supporting the importance of changes in histone octamer structure early in ISW2 remodeling. Transient octamer distortions are stabilized by H3-H4 tetramer disulfide crosslinking, thereby linking intrinsic histone octamer flexibility to chromatin remodeling.

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