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Architectural Proteins and Pluripotency Factors Cooperate to Orchestrate the Transcriptional Response of hESCs to Temperature Stress.

Authors
  • Lyu, Xiaowen1
  • Rowley, M Jordan1
  • Corces, Victor G2
  • 1 Department of Biology, Emory University, Atlanta, GA 30322, USA.
  • 2 Department of Biology, Emory University, Atlanta, GA 30322, USA. Electronic address: [email protected]
Type
Published Article
Journal
Molecular cell
Publication Date
Sep 20, 2018
Volume
71
Issue
6
Identifiers
DOI: 10.1016/j.molcel.2018.07.012
PMID: 30122536
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Cells respond to temperature stress via up- and downregulation of hundreds of genes. This process is thought to be regulated by the heat shock factor HSF1, which controls the release of RNAPII from promoter-proximal pausing. Here, we analyze the events taking place in hESCs upstream of RNAPII release. We find that temperature stress results in the activation or decommissioning of thousands of enhancers. This process involves alterations in the occupancy of transcription factors HSF1, AP-1, NANOG, KLF4, and OCT4 accompanied by nucleosome remodeling by BRG1 and changes in H3K27ac. Furthermore, redistribution of RAD21 and CTCF results in the formation and disassembly of interactions mediated by these two proteins. These alterations tether and untether enhancers to their cognate promoters or refashion insulated neighborhoods, thus transforming the landscape of enhancer-promoter interactions. Details of the 3D interactome remodeling process support loop extrusion initiating at random sites as a mechanism for the establishment of CTCF/cohesin loops. Copyright © 2018 Elsevier Inc. All rights reserved.

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