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Journal ArticleDOI

The language of covalent histone modifications.

Brian D. Strahl, +1 more
- 06 Jan 2000 - 
- Vol. 403, Iss: 6765, pp 41-45
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TLDR
It is proposed that distinct histone modifications, on one or more tails, act sequentially or in combination to form a ‘histone code’ that is, read by other proteins to bring about distinct downstream events.
Abstract
Histone proteins and the nucleosomes they form with DNA are the fundamental building blocks of eukaryotic chromatin. A diverse array of post-translational modifications that often occur on tail domains of these proteins has been well documented. Although the function of these highly conserved modifications has remained elusive, converging biochemical and genetic evidence suggests functions in several chromatin-based processes. We propose that distinct histone modifications, on one or more tails, act sequentially or in combination to form a 'histone code' that is, read by other proteins to bring about distinct downstream events.

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Citations
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Common themes in mechanisms of gene silencing.

TL;DR: The assembly of DNA into regions of inaccessible Chromatin, called silent chromatin, is involved in the regulation of gene expression and maintenance of chromosome stability in eukaryotes and recent studies on Sir2-containing silencing complexes suggest a common mechanism for the assembly of these domains.
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Histone Deacetylase Activity Is Required for Embryonic Stem Cell Differentiation

TL;DR: Preservation of global histone deacetylation by treatment with trichostatin A prevents ES cell differentiation, and ES cells undergo functionally important global and gene‐specific remodeling of chromatin structure during in vitro differentiation.
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Histone deacetylase inhibitors upregulate death receptor 5/TRAIL-R2 and sensitize apoptosis induced by TRAIL/APO2-L in human malignant tumor cells

TL;DR: In this article, a combination of histone deacetylase inhibitors (HDACIs) and TRAIL was shown to increase DR5 mRNA and protein in a dose and time-dependent manner.
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Multiple facets of histone variant H2AX: a DNA double-strand-break marker with several biological functions

TL;DR: The authors will emphasize that, just as H2 AX phosphorylation signals chromatin alteration and serves the canonical function of recruiting DSB repair factors, so the modification of H2AX in contexts other than the DNA damage response may contribute towards creating a specific chromatin structure frame allowing ‘non-canonical’ functions to be carried out in different cell types.
Journal ArticleDOI

Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4.

TL;DR: The histone H3–H4 tetramer-disrupting activity of CIA/asF1 and the crystal structure of the CIA/ASF1–histone-H3-H4 dimer complex should give insights into mechanisms of both nucleosomes assembly/disassembly and nucleosome semi-conservative replication.
References
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Journal ArticleDOI

Crystal structure of the nucleosome core particle at 2.8 Å resolution

TL;DR: 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 a superhelix around it.
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Histone acetylation in chromatin structure and transcription

TL;DR: The amino termini of histones extend from the nucleosomal core and are modified by acetyltransferases and deacetylases during the cell cycle, which may direct histone assembly and help regulate the unfolding and activity of genes.
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Protein modules and signalling networks

TL;DR: This work highlights conserved protein domains that act as key regulatory participants in many of these different signalling pathways in multicellular organisms.
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Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation.

TL;DR: It is proposed that the singular phosphorylation of the amino-terminus of histone H3 may be involved in facilitating two key functions during mitosis: (1) regulate protein-protein interactions to promote binding of trans-acting factors that “drive” chromatin condensation as cells enter M-phase and (2) coordinate chromatin decondensation associated with M- phase.
Journal ArticleDOI

Histone acetylation and transcriptional regulatory mechanisms

TL;DR: Understanding of the causal relationship between histone acetylation and gene expression has been enhanced dramatically by the identification of proteins with intrinsic hist one acetylase and deacetylase activity, which led to a major paradigm shift in understanding of chromatin structure and transcription regulation.
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