Structure and function of archaeal histones

The genomes of all organisms throughout the tree of life are compacted and organized in chromatin by association of chromatin proteins. Eukaryotic genomes encode histones, which are assembled on the genome into octamers, yielding nucleosomes. Post-translational modifications of the histones, which o...

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Bibliographic Details
Published in:PLoS genetics 2018-09, Vol.14 (9), p.e1007582-e1007582
Main Authors: Henneman, Bram, van Emmerik, Clara, van Ingen, Hugo, Dame, Remus T
Format: Article
Language:English
Subjects:
Archaea - physiology
Biology and life sciences
Chromatin
Crystallography, X-Ray
DNA
DNA - metabolism
Eukaryotes
Gene Expression Regulation, Archaeal - physiology
Genome, Archaeal - physiology
Histones - chemistry
Histones - physiology
Nucleosomes - metabolism
Physical Sciences
Review
RNA polymerases
Transcription, Genetic - physiology
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Summary:The genomes of all organisms throughout the tree of life are compacted and organized in chromatin by association of chromatin proteins. Eukaryotic genomes encode histones, which are assembled on the genome into octamers, yielding nucleosomes. Post-translational modifications of the histones, which occur mostly on their N-terminal tails, define the functional state of chromatin. Like eukaryotes, most archaeal genomes encode histones, which are believed to be involved in the compaction and organization of their genomes. Instead of discrete multimers, in vivo data suggest assembly of "nucleosomes" of variable size, consisting of multiples of dimers, which are able to induce repression of transcription. Based on these data and a model derived from X-ray crystallography, it was recently proposed that archaeal histones assemble on DNA into "endless" hypernucleosomes. In this review, we discuss the amino acid determinants of hypernucleosome formation and highlight differences with the canonical eukaryotic octamer. We identify archaeal histones differing from the consensus, which are expected to be unable to assemble into hypernucleosomes. Finally, we identify atypical archaeal histones with short N- or C-terminal extensions and C-terminal tails similar to the tails of eukaryotic histones, which are subject to post-translational modification. Based on the expected characteristics of these archaeal histones, we discuss possibilities of involvement of histones in archaeal transcription regulation.
ISSN:1553-7404
1553-7390
1553-7404
DOI:10.1371/journal.pgen.1007582