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Effects of the JADE-HBO1 complex on gene expression

ABSTRACT: We find that 499 genes are up-regulated and 457 are down-regulated in response to over-expression of JADE1, while 397 genes are up-regulated and 385 are down-regulated after HBO1 knock-down.

ORGANISM(S): Homo sapiens

PROVIDER: GSE33220 | GEO | 2012/03/15

SECONDARY ACCESSION(S): PRJNA156611

REPOSITORIES: GEO

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Effects of the JADE-HBO1 complex on gene expression

Project description:We find that 499 genes are up-regulated and 457 are down-regulated in response to over-expression of JADE1, while 397 genes are up-regulated and 385 are down-regulated after HBO1 knock-down. For each condition - HBO1 siRNA treatment or JADE1 over-expression - two biological replicates were analyzed in duplicate.

2012-03-15 | E-GEOD-33220 | biostudies-arrayexpress

Jade1 and the HBO1 complex are spatial-selective cofactors of Oct4

Project description:Oct4 is a master regulator of pluripotency. Potential Oct4 interactors have been cataloged extensively but the manner and significance of these interactions are incompletely defined. Like other POU domain proteins, Oct4 is capable of binding to DNA in multiple configurations, however the relationship between these configurations and cofactor recruitment (and hence transcription output) are unknown. Here, we show that Oct4 interacts with common and unique proteins when bound to DNA in different configurations. One of these proteins is Jade1, a component of the HBO histone acetyltransferase complex. Jade1 preferentially associates with Oct4 when bound to More palindromic Octamer-Related Element (MORE) DNA sequences that bind Oct4 dimers and are associated with strong gene expression. We show that the Oct4 N-terminus is critical for this interaction. ChIP-seq using HBO1, the enzymatic component of the complex, identifies a preference for binding adjacent to Oct4 at MORE sites. Using purified recombinant proteins and nucleosome complexes, we show that the HBO1 complex acetylates histone H3K9 within nucleosomes more efficiently when Oct4 is co-bound to a MORE site. Histone acetylation is further increased when Oct4 is mutated to favor dimeric MORE binding. Cryo-electron microscopy reveals that Oct4 bound to a MORE near the nucleosome entry/exit site partially unwinds DNA from nucleosome core particles, and identifies additional mass associated with the HBO1 complex. These results identify a novel mechanism of transcriptional regulation by Oct4.

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Jade1 and the HBO1 complex are spatial-selective cofactors of Oct4

Project description:Jade1 and the HBO1 complex are spatial-selective cofactors of Oct4

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HBO1 Catalyzes Lysine Benzoylation in Mammalian Cells

Project description:Lysine benzoylation (Kbz) is a newly discovered protein post-translational modification (PTM). This PTM can be stimulated by benzoate and contributes to gene expression. However, its regulatory enzymes and substrate proteins remain largely unknown, hindering further functional studies. Here we identified and validated the lysine acetyltransferase (KAT) HBO1 as a “writer” of Kbz in mammalian cells. In addition, we report the first benzoylome in mammalian cells, identifying 1747 Kbz sites, among them at least 77 are the HBO1-targeted Kbz substrates. Bioinformatics analysis showed that HBO1-targeted Kbz sites were involved in multiple processes, including chromatin remodeling, transcription regulation, immune regulation, and tumor growth. Our results thus identify key regulatory elements of the Kbz pathway, and reveal new enzymatic activity and functions of HBO1 in cellular physiology.

2022-10-14 | PXD034187 | Pride

Genome-wide map of HBO1 in cancer derived human cell line

Project description:We used ChIP-seq technology in order to map chromatin binding sites of the HBO1 MYST complex in the RKO cell line. We obtained a significant enrichment of the HBO1 signal right after TSS regions of genes and also In the proximal promoter region, with no signal on TSS. This enrichment also correlates with gene expression level. HBO1 signal in RKO cell line.

2012-03-15 | E-GEOD-33007 | biostudies-arrayexpress

Histone acetylation by HBO1 activates Wnt/β-catenin signaling to promote leukemogenesis in B-cell acute lymphoblastic leukemia

Project description:To investigate the underlying mechanism by which HBO1 promotes B-ALL progression, we established NALM-6 cell lines in which HBO1 has been knocked down by shRNA. We then performed gene expression profiling analysis of NALM-6/shHBO1 cells.

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HBO1 catalyzes lysine lactylation and mediates histone H3K9la to regulate gene transcription

Project description:Lysine lactylation (Kla) links metabolism and gene regulation and plays a key role in multiple biological processes. However, the regulatory mechanism and functional consequence of Kla remain to be explored. Here, we report that HBO1 functions as a lysine lactyltransferase to regulate transcription. Interestingly, CUT&Tag assays demonstrate that HBO1 is required for histone H3K9la on TSSs and the regulated Kla can facilitate in signaling pathways and progress of tumorigenesis. Our study reveals HBO1 serves as a lactyltransferase to mediate a histone Kla-dependent gene transcription.

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Project description:To determine the role of HBO1 in EC physiology, gene expression analysis was conducted on control and HBO1 siRNA-treated HUVECs. A total of 263 differentially regulated protein-coding transcripts were detected, many of which are key for growth and angiogenesis. Additionally, many genes involved in cell cycle, cell division, and DNA replication were dysregulated. HBO1-regulated genes were verified by qRT-PCR, including those with roles in vessel tone regulation (e.g. ACE1), vessel formation (e.g. CXCL16), EC activation (e.g. E-selectin), and cholesterol efflux (e.g. ABCG1).

2018-01-19 | GSE93608 | GEO

Jade1 and the HBO1 complex are spatial-selective cofactors of Oct4

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NUP98-HBO1-induced gene signature in human CB CD34+ cells

Project description:Chronic myelomonocytic leukemia (CMML) is an incurable hematopoietic stem cell malignancy. We identified a novel NUP98-HBO1 fusion from a patient with CMML. HBO1, a histone acetyltransferase (HAT) which belongs to the MYST family, is the first NUP98 fusion partner encodes HAT. To determine the effect of the NUP98-HBO1 fusion on downstream target gene regulation, we performed gene expression array analysis of NUP98-HBO1-transduced human cord blood (CB) CD34+ cells.

2019-03-13 | GSE112909 | GEO

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