Phylogenomics of the nucleosome
Top Cited Papers
- 28 October 2003
- journal article
- review article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 10 (11) , 882-891
- https://doi.org/10.1038/nsb996
Abstract
Histones are best known as the architectural proteins that package the DNA of eukaryotic organisms, forming octameric nucleosome cores that the double helix wraps tightly around. Although histones have traditionally been viewed as slowly evolving scaffold proteins that lack diversification beyond their abundant tail modifications, recent studies have revealed that variant histones have evolved for diverse functions. H2A and H3 variants have diversified to assume roles in epigenetic silencing, gene expression and centromere function. Such diversification of histone variants and 'deviants' contradicts the perception of histones as monotonous members of multigene families that indiscriminately package and compact the genome. How these diverse functions have evolved from ancestral forms can be addressed by applying phylogenetic tools to increasingly abundant sequence data.Keywords
This publication has 69 references indexed in Scilit:
- An ancestral nuclear protein assembly: Crystal structure of the Methanopyrus kandleri histoneProtein Science, 2001
- Genome sequence of Halobacterium species NRC-1Proceedings of the National Academy of Sciences, 2000
- Crystal structures of recombinant histones HMfA and HMfB from the hyperthermophilic archaeon Methanothermus fervidusJournal of Molecular Biology, 2000
- Diversity of prokaryotic chromosomal proteins and the origin of the nucleosomeCellular and Molecular Life Sciences, 1998
- Evidence for an early prokaryotic origin of histones H2A and H4 prior to the emergence of eukaryotesNucleic Acids Research, 1998
- Archaeal nucleosomesProceedings of the National Academy of Sciences, 1997
- Crystal structure of the nucleosome core particle at 2.8 Å resolutionNature, 1997
- Growth-phase-dependent synthesis of histones in the archaeon Methanothermus fervidus.Proceedings of the National Academy of Sciences, 1994
- DNA binding by the archaeal histone HMf results in positive supercoiling.Proceedings of the National Academy of Sciences, 1991
- HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones.Proceedings of the National Academy of Sciences, 1990