Homo sapiens
Ontology highlight
ABSTRACT:
PROVIDER: PRJDB14995 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| DRR426544_1.fastq.gz | Fastqsanger.gz | |||
| DRR426544_2.fastq.gz | Fastqsanger.gz | |||
| DRR426545_1.fastq.gz | Fastqsanger.gz | |||
| DRR426545_2.fastq.gz | Fastqsanger.gz | |||
| DRR426546_1.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 12 |
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Project description:Genomic localization of MOZ mutant proteins in HEK293T cells
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Project description:ENL is mutated in both Wilms tumor and leukemia which are the two major types of childhood cancers that occur at an early age. This study demonstrates that ENL mutants promote the loading of the DOT1L complex onto promoters in a MOZ/MORF histone acetyltransferase- dependent manner. The ENL protein is an epigenetic hub that interacts with multiple functionally distinct protein complexes to regulate transcription. MOZ binds to ENL through its YEATS domain to form a MOZ/ENL complex, which further recruits a DOT1L/AF10 complex and loads the ENL/DOT1L/AF10 complex onto nearby chromatin. Small indels in the YEATS domain increase the affinity to MOZ/MORF, which potentiates the interaction with ENL and the loading of the DOT1L complex, thereby hyperactivating HOX gene expression in embryonic kidney cells and hematopoietic cells. This oncogenic transformation can be suppressed by inhibitors of the histone-modifying activities of MOZ/MORF and DOT1L, paving the way for molecular targeted therapies against ENL-mutated cancers.
2025-07-05 | PXD053676 | JPOST Repository
Project description:Genomic localization of FLAG-tagged WH1 of MOZ and MORF in HEK293T cells
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Project description:Genomic localization of ENL, RNA Polymerase II, Histone H3K27ac in HEK293T and P31/FUJ cells.
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Project description:Genomic localization of H3K14ac marks in HEK293T cells
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Project description:Genomic localization of FLAG-tagged PHF16 and its PZP domain-deletion mutant in HEK293T cells
| PRJDB15670 | ENA
Project description:Acute leukaemias are commonly caused by mutations that corrupt the transcriptional circuitry of haematopoietic stem/progenitor cells. However, the mechanisms underlying large-scale transcriptional reprogramming remain largely unknown. Here we investigated transcriptional reprogramming at genome-scale in mouse retroviral transplant models of acute myeloid leukaemia (AML) using both gene-expression profiling and ChIP-sequencing. We identified several thousand candidate regulatory regions with altered levels of histone acetylation which were characterised by differential distribution of consensus motifs for key haematopoietic transcription factors. The integrated genome-scale analysis applied in this study represents a valuable and widely applicable approach to study the transcriptional control of both normal and aberrant haematopoiesis and to identify critical factors responsible for transcriptional reprogramming in human cancer. To monitor global expression changes during leukaemia progression for both MLL-ENL and MOZ-TIF1, we performed gene expression profiling for three biological replicates each of the lin-/kit+ bone marrow (WT), Factor-Dependent Cells Patterson-Mix cells (FDCP), MLL-ENL initiation (ME-I), MOZ-TIF2 initiation (MT-I), MLL-ENL progression (ME-L) and MOZ-TIF2 progression (MT-L) samples. Biotin-labelled cRNA from three biological replicates was generated from 250ng of total RNA and hybridized onto MouseWG-6 version 2 Expression Bead Chips.
2011-02-17 | E-GEOD-25539 | biostudies-arrayexpress
Project description:Gene expression profiling of immortalized human mesenchymal stem cells with hTERT/E6/E7 transfected MSCs. hTERT may change gene expression in MSCs. Goal was to determine the gene expressions of immortalized MSCs.
2010-09-25 | GSE24338 | GEO
Project description:Monocytic leukemia Zinc finger protein (MOZ) is a MYST-type acetyltransferase involved in chromosomal translocation in acute myelogenous leukemia (AML) and myelodysplastic syndrome. MOZ is established as essential for hematopoiesis; however, the role of MOZ in AML has not been addressed. We propose that MOZ is critical for AML development induced by MOZ-TIF2 fusions. Moz-deficient hematopoietic stem/progenitor cells (HSPCs) expressing MOZ-TIF2 could form colonies in vitro but could not induce AML in mice. By contrast, Moz was dispensable for colony formation by HOXA9-transduced cells and AML development caused by HOXA9 and MEIS1, suggesting a specific requirement for MOZ in AML induced by MOZ/MLL-fusions. Expression of the of Meis1, but not Hoxa9, was reduced in Moz-deficient MOZ-TIF2 AML cells. AML development induced by MOZ-TIF2 was rescued by introducing Meis1 into Moz-deficient cells carrying MOZ-TIF2. Meis1 deletion impaired MOZ-TIF2-mediated AML development. Active histone modifications were also severely reduced at the Meis1 locus in Moz-deficient MOZ-TIF2 AML cells. These results suggest that endogenous MOZ is critical for MOZ-fusion-induced AML development and maintains active chromatin signatures at target gene loci.
2022-07-24 | GSE208741 | GEO
Project description:Kynureninase is a member of a large family of catalytically diverse but structurally homologous pyridoxal 5'-phosphate (PLP) dependent enzymes known as the aspartate aminotransferase superfamily or alpha-family. The Homo sapiens and other eukaryotic constitutive kynureninases preferentially catalyze the hydrolytic cleavage of 3-hydroxy-l-kynurenine to produce 3-hydroxyanthranilate and l-alanine, while l-kynurenine is the substrate of many prokaryotic inducible kynureninases. The human enzyme was cloned with an N-terminal hexahistidine tag, expressed, and purified from a bacterial expression system using Ni metal ion affinity chromatography. Kinetic characterization of the recombinant enzyme reveals classic Michaelis-Menten behavior, with a Km of 28.3 +/- 1.9 microM and a specific activity of 1.75 micromol min-1 mg-1 for 3-hydroxy-dl-kynurenine. Crystals of recombinant kynureninase that diffracted to 2.0 A were obtained, and the atomic structure of the PLP-bound holoenzyme was determined by molecular replacement using the Pseudomonas fluorescens kynureninase structure (PDB entry 1qz9) as the phasing model. A structural superposition with the P. fluorescens kynureninase revealed that these two structures resemble the "open" and "closed" conformations of aspartate aminotransferase. The comparison illustrates the dynamic nature of these proteins' small domains and reveals a role for Arg-434 similar to its role in other AAT alpha-family members. Docking of 3-hydroxy-l-kynurenine into the human kynureninase active site suggests that Asn-333 and His-102 are involved in substrate binding and molecular discrimination between inducible and constitutive kynureninase substrates.
| S-EPMC2531291 | biostudies-literature