An alternative beads-on-a-string chromatin architecture in Thermococcus kodakarensis

EMBO Rep. 2013 Aug;14(8):711-7. doi: 10.1038/embor.2013.94. Epub 2013 Jul 9.

Abstract

We have applied chromatin sequencing technology to the euryarchaeon Thermococcus kodakarensis, which is known to possess histone-like proteins. We detect positioned chromatin particles of variable sizes associated with lengths of DNA differing as multiples of 30 bp (ranging from 30 bp to >450 bp) consistent with formation from dynamic polymers of the archaeal histone dimer. T. kodakarensis chromatin particles have distinctive underlying DNA sequence suggesting a genomic particle-positioning code and are excluded from gene-regulatory DNA suggesting a functional organization. Beads-on-a-string chromatin is therefore conserved between eukaryotes and archaea but can derive from deployment of histone-fold proteins in a variety of multimeric forms.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / genetics
  • Archaeal Proteins / metabolism
  • DNA, Archaeal / chemistry*
  • DNA, Archaeal / genetics
  • DNA, Archaeal / metabolism
  • Genome, Archaeal*
  • Histones / chemistry*
  • Histones / genetics
  • Histones / metabolism
  • Nucleic Acid Conformation
  • Nucleosomes / chemistry*
  • Nucleosomes / genetics
  • Nucleosomes / metabolism
  • Protein Folding
  • Protein Multimerization
  • Thermococcus / genetics*
  • Thermococcus / metabolism

Substances

  • Archaeal Proteins
  • DNA, Archaeal
  • Histones
  • Nucleosomes