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

• Published in: EMBO reports Vol. 14; no. 8; pp. 711 - 717
• Main Authors: Maruyama, Hugo, Harwood, Janet C, Moore, Karen M, Paszkiewicz, Konrad, Durley, Samuel C, Fukushima, Hisanori, Atomi, Haruyuki, Takeyasu, Kunio, Kent, Nicholas A
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01-08-2013; Nature Publishing Group UK; Blackwell Publishing Ltd; Nature Publishing Group
• Subjects: Archaea; Archaeal Proteins - chemistry; Archaeal Proteins - genetics; Archaeal Proteins - metabolism; Chromatin; chromatin-seq; Deoxyribonucleic acid; DNA; DNA, Archaeal - chemistry; DNA, Archaeal - genetics; DNA, Archaeal - metabolism; EMBO09; EMBO15; Genome, Archaeal; histone; Histones - chemistry; Histones - genetics; Histones - metabolism; Nucleic Acid Conformation; nucleosome; Nucleosomes - chemistry; Nucleosomes - genetics; Nucleosomes - metabolism; Polymers; Protein Folding; Protein Multimerization; Proteins; Scientific Report; Scientific Reports; Thermococcus; Thermococcus - genetics; Thermococcus - metabolism; nucleosome; histone; chromatin; chromatin‐seq; archaea
• ISSN: 1469-221X; 1469-3178
• DOI: 10.1038/embor.2013.94

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.
Chromatin‐sequencing reveals an archaeal histone‐protein based chromatin architecture, in which the beads‐on‐a‐string vary in size and associate with DNA lengths of 30bp or multiples thereof.