Conserved Molecular Interactions within the HBO1 Acetyltransferase Complexes Regulate Cell Proliferation

@article{Avvakumov2011ConservedMI,
  title={Conserved Molecular Interactions within the HBO1 Acetyltransferase Complexes Regulate Cell Proliferation},
  author={N. Avvakumov and M. Lalonde and N. Saksouk and E. Paquet and K. Glass and Anne-Julie Landry and Y. Doyon and Christelle Cayrou and G. Robitaille and D. Richard and Xiang-Jiao Yang and T. Kutateladze and J. C{\^o}t{\'e}},
  journal={Molecular and Cellular Biology},
  year={2011},
  volume={32},
  pages={689 - 703}
}
Acetyltransferase complexes of the MYST family with distinct substrate specificities and functions maintain a conserved association with different ING tumor suppressor proteins. [...] Key Result We show 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
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
Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2
TLDR
It is demonstrated that BRPF2 can regulate the H AT activity of HBO1 toward free H3 and H4, and nucleosomal H3, which provides new mechanistic insights into the regulation of the HAT activityof HBO1 by BRPF1. Expand
Structural and mechanistic insights into regulation of HBO 1 histone acetyltransferase activity by BRPF 2
HBO1, a member of the MYST family of histone acetyltransferases (HATs), is required for global acetylation of histone H3K14 and embryonic development. It functions as a catalytic subunit inExpand
The Tumor Suppressor ING5 Is a Dimeric, Bivalent Recognition Molecule of the Histone H3K4me3 Mark.
TLDR
It is observed that ING5 can form heterodimers with the highly homologous ING4, and that two of three primary tumor-associated mutants in the N-terminal domain strongly destabilize the coiled-coil structure, suggesting a driver role in cancer progression. Expand
Insights Into the Function of the NuA4 Complex in Plants
Chromatin remodeling plays a key role in the establishment and maintenance of gene expression patterns essential for plant development and responses to environmental factors. Post-translationalExpand
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
MOZ and MORF acetyltransferases: Molecular interaction, animal development and human disease.
TLDR
The human KAT 6A and KAT6B genes are recurrently mutated in leukemia, non-hematologic malignancies, and multiple developmental disorders displaying intellectual disability and various other abnormalities, therefore, these two acetyltransferases and their partner BRPF1 are important in animal development and human disease. Expand
Molecular Basis for the PZP Domain of BRPF1 Association with Chromatin.
TLDR
It is found that although both interactions of BRPF1PZP with the H3 tail and DNA are required for tight binding to NCP and for acetyltransferase function of theBRPF1-MORF-ING5-MEAF6 complex, binding to extranucleosomal DNA dominates. 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
HBO1-MLL interaction promotes AF4/ENL/P-TEFb-mediated leukemogenesis
Leukemic oncoproteins cause uncontrolled self-renewal of hematopoietic progenitors by aberrant gene activation, eventually causing leukemia. However, the molecular mechanism underlying aberrant geneExpand
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The NuA4 HAT complex is highly conserved in eukaryotes, in which it plays primary roles in transcription, cellular response to DNA damage, and cell cycle control. Expand
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Findings indicate that BRPF proteins play a key role in assembling and activating MOZ/MORF acetyltransferase complexes and enhances the transcriptional potential of MOZ and a leukemic MOZ-TIF2 fusion protein. Expand
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The function of MYST proteins in vivo is discussed, showing that some members of the MYST family are required for the development and self‐renewal of stem cell populations; other members are essential for the prevention of inappropriate heterochromatin spreading and for the maintenance of adequate levels of gene expression. Expand
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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
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HBO1 histone acetylase activity is essential for DNA replication licensing and inhibited by Geminin.
TLDR
H4 acetylation at origins by HBO1 is critical for replication licensing by Cdt1, and negative regulation of licensing by Geminin is likely to involve inhibition of HBO1 histone acetylase activity. Expand
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