The secret life of histones

@article{Rudolph2020TheSL,
  title={The secret life of histones},
  author={Johannes Rudolph and Karolin Luger},
  journal={Science},
  year={2020},
  volume={369},
  pages={33 - 33}
}
Histone H3 leads a double life as a copper reductase Histone proteins are the ubiquitous organizers of all eukaryotic genomes (1). Two each of the histones H2A, H2B, H3, and H4 form a disk-shaped assembly around which 147 base pairs (bp) of DNA are tightly coiled. Hundreds of thousands of these connected nucleosomes wrap up further to form chromosomes. The substantial sequence conservation between eukaryotic histones and the presence of simple histones in archaea (the presumed ancestors of all… Expand
2 Citations
Cu Homeostasis in Bacteria: The Ins and Outs
TLDR
This review summarizes the current knowledge on bacterial Cu homeostasis with a focus on Gram-negative bacteria and describes the multiple strategies that bacteria use for uptake, storage and export of Cu. Expand
The Metabolic-Epigenetic Nexus in Type 2 Diabetes Mellitus.
TLDR
This narrative review will comprehensively evaluate and detail the interplay between metabolism and epigenetic modifications in T2DM. Expand

References

SHOWING 1-10 OF 11 REFERENCES
The histone H3-H4 tetramer is a copper reductase enzyme
TLDR
A multifaceted approach ranging from in vitro biochemistry to in vivo genetic and molecular analyses found that the histone H3-H4 tetramer is an oxidoreductase enzyme that catalyzes reduction of cupric ions, thereby providing biologically usable cuprous ions for various cellular processes. Expand
Structure of histone-based chromatin in Archaea
TLDR
It is established that the histone-based mechanism of DNA compaction predates the nucleosome, illuminating the origin of the nucleOSome. Expand
Histone chaperones: assisting histone traffic and nucleosome dynamics.
TLDR
The importance of histone chaperones during development is discussed and how misregulation of the histone flow can link to disease is described, to show how they affect dynamics during DNA replication, DNA damage, and transcription, and how they maintain genome integrity. Expand
Old cogs, new tricks: the evolution of gene expression in a chromatin context
TLDR
The extent to which transcriptional regulatory components function in the context of the evolutionarily ancient role of chromatin as a barrier to processes acting on DNA is explored and how chromatin proteins have diversified to carry out evolutionarily recent functions that accompanied the emergence of differentiation and development in multicellular eukaryotes is discussed. Expand
Interactions of nickel(II) with histones. Stability and solution structure of complexes with CH3CO-Cys-Ala-Ile-His-NH2, a putative metal binding sequence of histone H3.
TLDR
Coordination of Ni(II) by the L motif in core histone H3 may be a key event in oxidative DNA base damage observed in the process of Ni (II)-induced carcinogenesis. Expand
Histones and metal-binding domains.
TLDR
Jeremy M. Berg describes potential metal-binding domains in nucleic acid-binding proteins and cites the fact that proteins known to bind ions have short sequences of the form Cys-X-Ala-Ile-His, which would generate a structure potentially able to coordinate a metal ion. Expand
Crystal structure of the nucleosome core particle at 2.8 Å resolution
The X-ray crystal structure of the nucleosome core particle of chromatin shows in atomic detail how the histone protein octamer is assembled and how 146 base pairs of DNA are organized into aExpand
A zinc‐finger like metal binding site in the nucleosome
UV spectroscopy demonstrated that chicken mononucleosomes bind Co(II) and Zn(II) ions at submicromolar concentrations in a tetrahedral mode, at a conserved zinc finger‐like site, composed of Cys110Expand
Structural Biology: Probing the Origins of Chromatin
A new study finds that archaeal histone dimers can multimerize into extended superhelical structures that mediate gene expression changes, providing possible insights into the transition toExpand
Structure of the nucleosome core particle at 7 Å resolution
TLDR
The crystal structure of the nucleosome core particle has been solved to 7 Å resolution and the central turn of superhelix and H3 · H4 tetramer have dyad symmetry, but the H2A · H2B dimers show departures due to interparticle associations. Expand
...
1
2
...