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Crosstalk between combinatorial histone H4 post-translational modifications influence ATAD2B bromodomain activity

ABSTRACT: Investigation of bromodomain activity of the ATPase family which contains ATAD2B. Specifically we explore the cross talk between histone H4 post translational modifications and their modulation of chromatin readers of the ATAD2B bromodomain

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Margaret Phillips

PROVIDER: MSV000091059 | MassIVE | Thu Jan 12 17:35:00 GMT 2023

REPOSITORIES: MassIVE

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Crosstalk between combinatorial histone H4 post-translational modifications influence ATAD2B bromodomain activity

Project description:Investigation of bromodomain activity of the ATPase family which contains ATAD2B. Specifically we explore the cross talk between histone H4 post translational modifications and their modulation of chromatin readers of the ATAD2B bromodomain

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Crosstalk between combinatorial histone H4 post-translational modifications influence ATAD2B bromodomain activity

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Dynamic competing histone H4 K5K8 acetylation and butyrylation are hallmarks of highly active gene promoters

Project description:Newly discovered histone lysine acylations increase the functional diversity of nucleosomes well beyond acetylation. Here, we focus on histone butyrylation in the context of sperm cell differentiation. Specifically, we investigate the butyrylation of histone H4 lysine 5 and 8 at gene promoters, where acetylation guides the binding of Brdt, a bromodomain-and-extra-terminal protein, thereby mediating stage-specific gene expression programs. Genome-wide mapping data show that highly active Brdt-bound gene promoters systematically harbour competing histone acetylation and butyrylation marks at H4 K5 and K8. Histone butyrylation, despite acting as a direct stimulator of transcription, competes with acetylation, especially at H4 K5, to prevent Brdt binding. The observed in vivo H4 K5K8 acetylation butyrylation state at active promoters is reproduced in vitro where p300 indistinctly acetylates and butyrylates H4 K5 and K8. Altogether, highly active gene promoter regions are characterized by alternating H4 acetylation and butyrylation sustaining direct gene activation and a dynamic bromodomain binding.

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Nut is a cell type-specific stimulator of p300 enhancing H4 hyperacetylation during haploid male genome programming

Project description:NUT, nuclear protein in testis is the universal fusion partner of BRD4 in the highly aggressive NUT Midline Carcinoma (NMC), but its physiological function is unknown. Here we show that Nut is exclusively expressed in post-meiotic spermatogenic cells, at the time of genome-wide histone hyperacetylation. Inactivation of Nut induces a spermatogenesis arrest at the histone-to-protamine replacement stage, leading to male infertility. Subsequent molecular investigations show that Nut sustains global histone H4 hyperacetylation in post-meiotic cells. Additionally, Nut mediates a p300/CBP-dependent gene expression program and, by enhancing acetylation of H4 at both K5 and K8 sites, provides binding sites for the first bromodomain of Brdt, which drives histone removal. Our results bring the first evidence of Nut’s function in spermatogenic cells where it uses the ubiquitous HATs p300/CBP to direct a cell-type specific histone H4 hyperacetylation. The ectopic activity of Nut in NMC recreates a forced p300-induced histone hyperacetylation / bromodomain-binding loop that normally operates in post-meiotic spermatogenic cells.

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Rhizobium sp. H4 strain:H4

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Fluctuations in histone H4 isoforms during cellular reprogramming monitored by middle-down proteomics

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Project description:To address a target gene spectrum of CpBV-H4, we need to analyze total gene expression in response to a specific expression of CpBV-H4 by a transient expression technique.

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Functional cooperation between AAA-ATPase domain and a bromodomain.

Project description:A functional cooperation between an AAA type ATPase domain and a bromodomain has been evidenced. These two domains were identified and their activity tested in a yet uncharacterized factor, named Atad2, whose two-domain configuration remained highly conserved during evolution. In human and mouse, Atad2 is most abundantly expressed in testis and in the mouse. It has also been detected in post-meiotic stages and in mature spermatozoa. The AAA-ATPase domain was found necessary for protein multimerization and high affinity binding to acetylated nucleosomes by its bromodomain. The binding was found specific to acetylated histone H4 tail with a critical role for the acetylated K5 position. In vivo studies show that Atad2 behaves as a general repressor of transcription and possesses a chromatin “freezing” activity. Finally, we demonstrate that the induction of apoptosis leads to an early degradation of Atad2, which probably facilitates the action of apoptotic factors by increasing chromatin dynamics.

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Nut directs p300-dependant genome-wide H4 hyperacetylation in male germ cells: transcriptomic data

Project description:NUT, nuclear protein in testis, is a universal oncogenic driver in the highly aggressive NUT Midline Carcinoma whose physiological function in male germ cells had so far remained unknown. Here we show that Nut’s expression is normally restricted to post-meiotic spermatogenic cells, where its presence triggers the p300-dependant genome-wide histone H4 hyperacetylation, which is essential for the completion of histone-to-protamine exchange. Accordingly, the inactivation of Nut induces male sterility with spermatogenesis arrest at the histone removal stage. Molecular investigations show that Nut uses CBP/p300 to enhance acetylation of H4 at both K5 and K8 providing binding sites for the first bromodomain of Brdt, the testis-specific member of the BET family, which subsequently mediates genome-wide histone removal. Altogether, our data reveal the detailed molecular basis of the global histone hyperacetylation wave, which has long been known to occur prior to the final compaction of the male genome.

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