Unexpected conformational variations of the human centromeric chromatin complex

Genes Dev. 2018 Jan 1;32(1):20-25. doi: 10.1101/gad.307736.117. Epub 2018 Jan 31.

Abstract

We combined classical salt fractionation with chromatin immunoprecipitation to recover human centromeric chromatin under native conditions. We found that >85% of the total centromeric chromatin is insoluble under conditions typically used for native chromatin extraction. To map both soluble and insoluble chromatin in situ, we combined CUT&RUN (cleavage under targets and release using nuclease), a targeted nuclease method, with salt fractionation. Using this approach, we observed unexpected structural and conformational variations of centromere protein A (CENP-A)-containing complexes on different α-satellite dimeric units within highly homogenous arrays. Our results suggest that slight α-satellite sequence differences control the structure and occupancy of the associated centromeric chromatin complex.

Keywords: centromeres; chromatin; methodology.

MeSH terms

  • Centromere / chemistry*
  • Centromere Protein A / chemistry*
  • Centromere Protein A / isolation & purification
  • Centromere Protein A / metabolism
  • Centromere Protein B / chemistry
  • Centromere Protein B / metabolism
  • Chemical Fractionation
  • Chromatin / chemistry*
  • Chromatin / isolation & purification
  • Chromatin Immunoprecipitation
  • Chromosomal Proteins, Non-Histone / chemistry
  • Chromosomal Proteins, Non-Histone / metabolism
  • DNA, Satellite / chemistry
  • Humans
  • K562 Cells
  • Solubility

Substances

  • CENPB protein, human
  • Centromere Protein A
  • Centromere Protein B
  • Chromatin
  • Chromosomal Proteins, Non-Histone
  • DNA, Satellite
  • centromere protein C