HBO1 HAT complexes target chromatin throughout gene coding regions via multiple PHD finger interactions with histone H3 tail.

@article{Saksouk2009HBO1HC,
  title={HBO1 HAT complexes target chromatin throughout gene coding regions via multiple PHD finger interactions with histone H3 tail.},
  author={N. Saksouk and N. Avvakumov and K. Champagne and T. Hung and Y. Doyon and Christelle Cayrou and E. Paquet and M. Ullah and Anne-Julie Landry and Val{\'e}rie C{\^o}t{\'e} and Xiang-Jiao Yang and O. Gozani and T. Kutateladze and J. C{\^o}t{\'e}},
  journal={Molecular cell},
  year={2009},
  volume={33 2},
  pages={
          257-65
        }
}
The HBO1 HAT protein is the major source of histone H4 acetylation in vivo and has been shown to play critical roles in gene regulation and DNA replication. A distinctive characteristic of HBO1 HAT complexes is the presence of three PHD finger domains in two different subunits: tumor suppressor proteins ING4/5 and JADE1/2/3. Biochemical and functional analyses indicate that these domains interact with histone H3 N-terminal tail region, but with a different specificity toward its methylation… Expand
Exchange of associated factors directs a switch in HBO1 acetyltransferase histone tail specificity.
TLDR
A crucial new role for associated proteins within HAT complexes, previously thought to be intrinsic to the catalytic subunit, is uncovered. Expand
Conserved Molecular Interactions within the HBO1 Acetyltransferase Complexes Regulate Cell Proliferation
TLDR
It is shown that natively regulated association of the ING4/5 PHD domain with HBO1-JADE determines the growth inhibitory function of the complex, linked to its tumor suppressor activity. Expand
Deciphering structure, function and mechanism of lysine acetyltransferase HBO1 in protein acetylation, transcription regulation, DNA replication and its oncogenic properties in cancer
TLDR
The understanding of the multiple functions, activity regulation, and disease relationship of HBO1 is discussed and the recent advances are reviewed. Expand
Dissecting the Molecular Basis of the Scaffold Protein JADE in HBO1 Histone Acetyltransferase (HAT) Activity
HBO1 is a member of the human MYST family of acetyltransferases that is evolutionarily conserved from yeast to human. HBO1 functions in the context of a multi-protein histone acetyltransferase (HAT)Expand
The scaffolding protein JADE1 physically links the acetyltransferase subunit HBO1 with its histone H3–H4 substrate
TLDR
It is demonstrated that HBO1 contains an N-terminal histone-binding domain (HBD) that makes additional contacts with H3–H4 independent of JADE1 interactions with histones and that the HBO1 HBD does not significantly contribute to HBO1's overall HAT activity. Expand
Chd5 requires PHD-mediated histone 3 binding for tumor suppression.
TLDR
This work defines Chd5 as an N-terminally unmodified H3-binding protein and provides functional evidence that this interaction orchestrates chromatin-mediated transcriptional programs critical for tumor suppression. Expand
Bivalent interaction of the PZP domain of BRPF1 with the nucleosome impacts chromatin dynamics and acetylation
TLDR
It is demonstrated that the DNA-binding function of the BRPF1 PZP domain is required for the MOZ-BRPF1-ING5-hEaf6 HAT complex to be recruited to chromatin and to acetylate nucleosomal histones, revealing a novel link between chromatin dynamics and MOz-mediated acetylation. Expand
Combinatorial readout of unmodified H3R2 and acetylated H3K14 by the tandem PHD finger of MOZ reveals a regulatory mechanism for HOXA9 transcription.
TLDR
The findings suggest that the combinatorial readout of the H3R2/K14ac by PHD12 might represent an important epigenetic regulatory mechanism that governs transcription and also provide a clue of cross-talk between the MOZ complex and histone H3 modifications. Expand
Chromatin Recognition Protein Modules: The PHD Finger
TLDR
This work characterised two classes among the PHD fingers, which specifically bind to either unmodified or trimethylated K4 histone H3, and revealed a number of PHD finger structures in complex with histone peptides reveal the recognition mechanisms. Expand
Depletion of PHF14, a novel histone-binding protein gene, causes neonatal lethality in mice due to respiratory failure.
TLDR
The aim of this study is to characterize PHF14 and investigate its biological significance by employing multiple approaches including mouse gene-targeting knockout, and molecular cloning and characterization, and co-immunoprecipitation results suggested that PHF 14α bound to histones via its PHD fingers. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 20 REFERENCES
The crystal structure of the ING5 PHD finger in complex with an H3K4me3 histone peptide
TLDR
Functional data are the first direct evidence supporting the critical role of ING5 in directing the MOZ/MORF and HBO1 complexes to chromatin, which consequently increases the local HAT activity and stimulates chromatin remodeling. Expand
ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression
TLDR
A novel class of methylated H3K4 effector domains—the PHD domains of the ING (for inhibitor of growth) family of tumour suppressor proteins—are identified and established a pivotal role for trimethylation of H 3K4 in gene repression and, potentially, tumour suppressing mechanisms. Expand
ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation.
TLDR
Since INGs, HBO1, and MOZ/MORF contribute to oncogenic transformation, the multisubunit assemblies characterized here underscore the critical role of epigenetic regulation in cancer development. Expand
Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2
TLDR
The structure of the mouse ING2 PHD finger in complex with a histone H3 peptide trimethylated at lysine 4 is reported and strong binding of other ING and YNG PHD fingers suggests that the recognition of H3K4me3 histone code is a general feature of the ING/YNG proteins. Expand
ING4 mediates crosstalk between histone H3 K4 trimethylation and H3 acetylation to attenuate cellular transformation.
TLDR
A mechanism for brokering crosstalk between H3K4 methylation and H3 acetylation is demonstrated and a molecular link between chromatin modulation and tumor suppressor mechanisms is revealed. Expand
Disruptor of Telomeric Silencing-1 Is a Chromatin-specific Histone H3 Methyltransferase*
TLDR
It is shown that the Dot1 protein possesses intrinsic histone methyltransferase activity, and it is demonstrated that, like its mammalian homolog PRMT1, Rmt1 specifically dimethylates an arginine residue at position 3 of histone H4 N-terminal tail. Expand
A comprehensive synthetic genetic interaction network governing yeast histone acetylation and deacetylation.
TLDR
The genetic interaction data unveil an underappreciated role of HDACs in maintaining cellular viability, and led to show that deacetylation of the histone variant Htz1p at Lys 14 is mediated by Hda1p, and new characterizations of the HDA and NuA4 complexes demonstrate how systematic analyses of genetic interactions may help illuminate the mechanisms of intricate cellular processes. Expand
Role of Jade-1 in the Histone Acetyltransferase (HAT) HBO1 Complex*♦
TLDR
It is demonstrated that Jade-1/1L are crucial co-factors for HBO1-mediated histone H4 acetylation in live cells and in vitro with reconstituted oligonucleosome substrates. Expand
The MYST family of histone acetyltransferases and their intimate links to cancer
TLDR
The histone acetyltransferases of the MYST family are highly conserved in eukaryotes and carry out a significant proportion of all nuclear acetylation, suggesting that anomalous activity of these HATs or their associated complexes can easily lead to severe cellular malfunction, resulting in cell death or uncontrolled growth and malignancy. Expand
HBO1 histone acetylase is a coactivator of the replication licensing factor Cdt1.
TLDR
HBO1 histone acetylase plays a direct role at replication origins as a coactivator of the Cdt1 licensing factor, and it enhancesCdt1-dependent rereplication. Expand
...
1
2
...