Diversity of prokaryotic chromosomal proteins and the origin of the nucleosome

  title={Diversity of prokaryotic chromosomal proteins and the origin of the nucleosome},
  author={Kathleen Sandman and Suzette L Pereira and John N. Reeve},
  journal={Cellular and Molecular Life Sciences CMLS},
Abstract. All cells employ architectural proteins to confine and organize their chromosomes, and to prevent the otherwise thermodynamically favored collapse of concentrated DNA into compact structures. To accomplish this, prokaryotes have evolved a variety of phylogenetically unrelated, small, basic, sequence-independent DNA-binding proteins that include histones in Euryarchaeota, and members of the HU family in many Bacteria. In contrast, virtually all Eukarya employ histones, and recently a… 
Archaeal Histone Contributions to the Origin of Eukaryotes.
Structure and function of archaeal histones
The amino acid determinants of hypernucleosome formation are discussed and differences with the canonical eukaryotic octamer are highlighted and possibilities of involvement of histones in archaeal transcription regulation are discussed.
Structure and functional relationships of archaeal and eukaryal histones and nucleosomes
A comparison of the properties of both nucleosomes in terms of DNA packaging and the accessibility of the packaged DNA for transcription is compared.
Phylogenomics of the nucleosome
Diversification of histone variants and 'deviants' contradicts the perception of histones as monotonous members of multigene families that indiscriminately package and compact the genome.
Prokaryotic and eukaryotic chromosomes: what's the difference?
  • A. J. Bendich, K. Drlica
  • Biology
    BioEssays : news and reviews in molecular, cellular and developmental biology
  • 2000
It is suggested that the criterion of nucleosome-based packaging of chromosomal DNA may be more useful than the prokaryote/eukaryote dichotomy for inferring the broadest phylogenetic relationships among organisms.
Novel clades of the HU/IHF superfamily point to unexpected roles in the eukaryotic centrosome, chromosome partitioning, and biologic conflicts
Evidence is presented that a novel eukaryotic clade prototyped by the human CCDC81 protein acquired roles beyond DNA-binding, likely in protein-protein interaction in centrosome organization and as a potential cargo-binding protein in conjunction with Dynein-VII.


Evidence for an early prokaryotic origin of histones H2A and H4 prior to the emergence of eukaryotes.
Sequence analyses indicate that the N-terminal repeat is most closely related to eukaryotic H2A and H4 histones, whereas the C-Terminal repeat resembles that found in prokaryotic histones which implies an early divergence within the histone gene family prior to the emergence of eukARYotes.
A comparison of the DNA binding properties of histone-like proteins derived from representatives of the two kingdoms of the Archaea
The nucleoid protein composition, the enhancement of DNA electrophoretic mobility, the toroidal wrapping and the helical period of DNA complexed with nucleoid proteins from species within the
Physiologically important stabilization of DNA by a prokaryotic histone-like protein.
It is suggested that the physiological function of the thermophilic mycoplasma Thermoplasma acidophilum is to prevent complete separation of the DNA strands during brief exposures of the organism to denaturing conditions, and thus to facilitate rapid renaturation when normal environmental conditions return.
DNA stability and DNA binding proteins.
Histonelike proteins of bacteria.
This work considers the protein called IHF to be histonelike because it can wrap DNA and because it has considerable amino acid sequence homology with HU, a small, basic, abundant, DNA-binding protein capable of wrapping DNA.
Archaebacterial histone-like protein MC1 can exhibit a sequence-specific binding to DNA.
The binding of MC1 protein to the region preceding the strongly expressed genes encoding methyl coenzyme reductase in a closely related micro-organism has been investigated and it is shown that the DNA bends upon MC1 binding.
HMf, a histone-related protein from the hyperthermophilic archaeon Methanothermus fervidus, binds preferentially to DNA containing phased tracts of adenines
HMf, a histone-related protein from Methanothermus fervidus, was found to bind preferentially to a DNA that is intrinsically bent as a result of the presence of phased oligo(dA) tracts. The
The hyperthermophile chromosomal protein Sac7d sharply kinks DNA
The crystal structure of Sac7d in complex with two DNA sequences to high resolution is solved and it is revealed thatSac7d binds in the minor groove, causing a sharp kinking of the DNA helix that is more marked than that induced by any sequence-specific DNA-binding proteins.
A protein structural motif that bends DNA
From the high‐resolution structure of HU, a model for this interaction with DNA is proposed andcial amino acid differences between the proteins can be rationalized in terms of their different specific functions.