OCT4 cooperates with distinct ATP-dependent chromatin remodelers in naïve and primed pluripotent states in human
Name
s41467-021-25107-3.pdf
Description
Published version
Size
6.32 MB
Format
Adobe PDF
Checksum (MD5)
fa5c3eadd5431f0b157baa1b731bb5ed
Author(s)
Huang, Xin
Park, Kyoung-mi
Gontarz, Paul
Zhang, Bo
Pan, Joshua
McKenzie, Zachary
Fischer, Laura A
Dong, Chen
Dietmann, Sabine
Xing, Xiaoyun
Date Issued
2021
Journal
Nature Communications
Publisher
Springer Science and Business Media LLC
Citation
Huang, Xin, Park, Kyoung-mi, Gontarz, Paul, Zhang, Bo, Pan, Joshua et al. 2021. "OCT4 cooperates with distinct ATP-dependent chromatin remodelers in naïve and primed pluripotent states in human." Nature Communications, 12 (1).
Version
Final published version
Abstract
AbstractUnderstanding the molecular underpinnings of pluripotency is a prerequisite for optimal maintenance and application of embryonic stem cells (ESCs). While the protein-protein interactions of core pluripotency factors have been identified in mouse ESCs, their interactome in human ESCs (hESCs) has not to date been explored. Here we mapped the OCT4 interactomes in naïve and primed hESCs, revealing extensive connections to mammalian ATP-dependent nucleosome remodeling complexes. In naïve hESCs, OCT4 is associated with both BRG1 and BRM, the two paralog ATPases of the BAF complex. Genome-wide location analyses and genetic studies reveal that these two enzymes cooperate in a functionally redundant manner in the transcriptional regulation of blastocyst-specific genes. In contrast, in primed hESCs, OCT4 cooperates with BRG1 and SOX2 to promote chromatin accessibility at ectodermal genes. This work reveals how a common transcription factor utilizes differential BAF complexes to control distinct transcriptional programs in naïve and primed hESCs.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Terms of Use
Creative Commons Attribution 4.0 International license
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1038/S41467-021-25107-3
