Mature chromatin packing domains persist after RAD21 depletion in 3D

Sci Adv. 2025 Jan 24;11(4):eadp0855. doi: 10.1126/sciadv.adp0855. Epub 2025 Jan 24.

Abstract

Understanding chromatin organization requires integrating measurements of genome connectivity and physical structure. It is well established that cohesin is essential for TAD and loop connectivity features in Hi-C, but the corresponding change in physical structure has not been studied using electron microscopy. Pairing chromatin scanning transmission electron tomography with multiomic analysis and single-molecule localization microscopy, we study the role of cohesin in regulating the conformationally defined chromatin nanoscopic packing domains. Our results indicate that packing domains are not physical manifestation of TADs. Using electron microscopy, we found that only 20% of packing domains are lost upon RAD21 depletion. The effect of RAD21 depletion is restricted to small, poorly packed (nascent) packing domains. In addition, we present evidence that cohesin-mediated loop extrusion generates nascent domains that undergo maturation through nucleosome posttranslational modifications. Our results demonstrate that a 3D genomic structure, composed of packing domains, is generated through cohesin activity and nucleosome modifications.

MeSH terms

  • Animals
  • Cell Cycle Proteins* / genetics
  • Cell Cycle Proteins* / metabolism
  • Chromatin* / genetics
  • Chromatin* / metabolism
  • Chromosomal Proteins, Non-Histone* / chemistry
  • Chromosomal Proteins, Non-Histone* / genetics
  • Chromosomal Proteins, Non-Histone* / metabolism
  • Cohesins*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Humans
  • Nucleosomes / metabolism
  • Nucleosomes / ultrastructure
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism
  • Protein Processing, Post-Translational

Substances

  • Cell Cycle Proteins
  • Chromatin
  • Chromosomal Proteins, Non-Histone
  • Cohesins
  • DNA-Binding Proteins
  • Nucleosomes
  • RAD21 protein, human
  • Phosphoproteins