Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Proline hydroxylation of ChREBP

ABSTRACT: This project investigated proline hydroxylation of ChREBP. Proline hydroxylation was investigated in flag-IP enriched protein extracts from ChREBP-flag overexpressing HEK293 cells (A) and in ChREBP-IP enriched mouse liver protein (male, C57BL6/J) (B).

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Liver

SUBMITTER: Michael Schupp

LAB HEAD: Michael Schupp

PROVIDER: PXD019137 | Pride | 2020-10-19

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	HEKsampleMascotSearchResultsQ99MZ3.htm	Other
	MS619_HS447_3_HEK293_A.raw	Raw
	MS683_HS473_D_mouse_liver_B.raw	Raw
	mouseliverMascotSearchResultsQ99MZ3.htm	Other

Items per page:

1 - 4 of 4

Publications

The glucose-sensing transcription factor ChREBP is targeted by proline hydroxylation.

Heidenreich Steffi S Weber Pamela P Stephanowitz Heike H Petricek Konstantin M KM Schütte Till T Oster Moritz M Salo Antti M AM Knauer Miriam M Goehring Isabel I Yang Na N Witte Nicole N Schumann Anne A Sommerfeld Manuela M Muenzner Matthias M Myllyharju Johanna J Krause Eberhard E Schupp Michael M

The Journal of biological chemistry 20201006 50

Cellular energy demands are met by uptake and metabolism of nutrients like glucose. The principal transcriptional regulator for adapting glycolytic flux and downstream pathways like <i>de novo</i> lipogenesis to glucose availability in many cell types is carbohydrate response element-binding protein (ChREBP). ChREBP is activated by glucose metabolites and post-translational modifications, inducing nuclear accumulation and regulation of target genes. Here we report that ChREBP is modified by prol ...[more]

PMID: 33023907

Similar Datasets

RNA-sequencing of human cervical cancer HeLa cells treated with splicing inhibitors Sudemycin C1, Sudemycin K, Spliceostatin A or control DMSO.

Project description:HeLa cells were co-treated with the drugs or DMSO control and BrU. After 3 hours, cells were harvested. Both total RNA and recently transcribed RNA (isolated by BrU immunoprecipitation) were sequenced.

2017-10-29 | E-MTAB-6060 | biostudies-arrayexpress

PHD3 and FIH substrates cluster in distinct signalling pathways

Project description:Amino acid hydroxylation is a common post-translational modification which regulates intra and inter-molecular protein-protein interactions. The modifications are regulated by a family of 2-oxoglutarate (2OG) dependent enzymes and although the biochemistry is well understood, until now only a few substrates have been described for these enzymes. We present here a sensitive method which specifically enriches and identifies hydroxylase substrates. We screened for substrates of PHD3 and FIH, a proline and asparagine hydroxylase respectively which regulate the HIF-mediated hypoxic response and were able to confirm known substrates as well as identifying hundreds of potential novel ones. Enrichment analysis revealed that the substrates of both hydroxylases cluster in the same pathways but frequently modify different nodes of these networks. We confirm that two proteins identified in this screen, MAPK6 and RIPK4, are indeed hydroxylated in a FIH or PHD3 dependent mechanism and explore the biological consequences of the hydroxylation.

2016-03-30 | PXD001085 | Pride

Histone H3 proline 16 hydroxylation regulates mammalian gene expression

Project description:Histone H3 proline 16 hydroxylation regulates mammalian gene expression

| PRJNA742234 | ENA

Transcriptome-wide identification of Hfq-associated RNAs in Brucella suis by deep sequencing

Project description:We report the identification of new noncoding RNAs in Brucella suis 1330 and that are associated to the chaperone protein Hfq Coimmunoprecipitation using Flag-tagged Hfq as bait

2015-11-25 | E-GEOD-73621 | biostudies-arrayexpress

Hydroxylation of 5-methylcytosine by TET2 maintains the active state of the mammalian HOXA cluster

Project description:This SuperSeries is composed of the following subset Series: GSE32362: Hydroxylation of 5-methylcytosine by TET2 maintains the active state of the mammalian HOXA cluster (Illumina HumanMethylation450 BeadChip) GSE33129: Hydroxylation of 5-methylcytosine by TET2 maintains the active state of the mammalian HOXA cluster (Illumina HiSeq2000 sequencing) Refer to individual Series

2012-05-02 | E-GEOD-33130 | biostudies-arrayexpress

ChIP-seq of E. coli to identify H-NS and Fis binding at multiple time-points during growth in rich medium

Project description:Among the most important regulators of gene expression in bacteria are 'nucleoid-associated proteins'. These proteins alter the topology of the bound DNA by bending, wrapping or bridging it, thus having multiple effects, including transcriptional regulation, on the bacterial cell. Among the best-studied nucleoid proteins are H-NS and Fis, which bind to specific sequences on the DNA. H-NS is a global repressor of gene expression. Fis alters the global conformation of the DNA by introducing branched structures in it; but its effect on gene expression on a genomic scale remains largely unclear.<br><br>Several bacterial transcriptional regulators including H-NS and Fis have been studied using ChIP-chip. However, the higher resolution and dynamic range offered by ChIP-Seq have not been exploited for any bacterial species. By performing ChIP-Seq of these two proteins, we present the first such study in a bacterium. In addition to providing a proof-of-principle for the use of this technology for bacteria, we perform our study at multiple time-points during growth in rich medium, thus generating new insights into how these proteins function under different cellular conditions. Further, by analysing our data in conjunction with newly-generated gene expression and RNA polymerase-chromosome interaction data we provide new interpretation of the genome-scale patterns of the interactions of these proteins to the DNA.

2010-09-01 | E-MTAB-332 | biostudies-arrayexpress

Immunoprecipitation of RNA-DNA hybrid interacting proteins in Trypanosoma brucei reveals conserved and novel activities, including in host immune evasion by antigenic variation

Project description:RNA-DNA hybrids are widespread epigenetic features of genomes that provide a growing range of activities in transcription, chromatin and DNA replication and repair. Understanding of these diverse functions has been advanced by characterising the proteins that interact with the hybrids, with all such studies revealing hundreds of potential interactors. However, all interaction analyses to date have focused on mammalian cells, and so it is unclear if a similar spectrum of RNA-DNA hybrid interactors found in other eukaryotes, thus limiting our understanding of the conserved and lineage-specific activities linked to these genetic structures. The African trypanosome is a compelling organism in which to address these questions. As a divergent single-cell eukaryotic parasite of the Discoba grouping, Trypanosoma brucei displays substantial divergence in several aspects of core biology from its mammalian host and, unusually for a protist, has well-developed tools for molecular genetic analysis. For these reasons, we used DNA-RNA hybrid immunoprecipitation coupled with mass spectrometry to reveal 602 putative interactors in T. brucei mammal- or insect vector-infective stage cells. We show that the approach selects for a subset of the parasite proteome and reveals a range of predicted RNA-DNA hybrid associated activities, some overlapping with similar studies in mammals. We demonstrate that loss of three factors, two putative helicases and a RAD51 paralogue, impact on T. brucei nuclear RNA-DNA hybrid and DNA damage levels. Moreover, loss of each affects the operation of the crucial parasite immune survival mechanism of antigenic variation. Thus, our work reveals the broad range of activities contributed by RNA-DNA hybrids to T. brucei biology, including new functions in host immune evasion as well as many conserved with mammals, and so likely fundamental to eukaryotic genome function.

2024-01-26 | PXD042146 | Pride

Lack of activity of recombinant HIF prolyl hydroxylases (PHDs) on reported non-HIF substrates

Project description:Hypoxia Inducible Factor (HIF) prolyl hydroxylase domain (PHD) enzymes catalyse the posttranslational hydroxylation of conserved prolyl residues in the alpha-subunit of the HIF transcription factor. These modifications, which promote the degradation of HIF-alpha subunits by the pVHL E3 ligase complex and impart oxygen-dependent regulation of the HIF transcriptional response, have been extensively characterised at the molecular, cellular and organismal level. Since the discovery of the PHDs, a range of less well-characterised non-HIF substrates have been reported with the potential to confer oxygen-sensitivity to a diverse range of cellular processes. We sought to systematically compare all of the reported non-HIF substrates for their ability to support PHD-catalysed hydroxylation. We performed a comprehensive series of in vitro hydroxylation assays reacting synthetic peptides and full-length protein substrates generated by in vitro transcription and translation with purified recombinant enzyme preparations. Prolyl hydroxylation was assayed directly by mass spectrometry and radiochemical assay for hydroxyproline. Both methods enabled quantitative appraisal of enzyme-catalysed hydroxylation, with liquid chromatography mass spectrometry methods employing NMR-quantified peptide standards to calibrate retention time signatures and determine ionisation efficiencies for each target peptide. Using these approaches we assayed hydroxylation on 23 different proteins. Surprisingly, we did not detect measurable hydroxylation on any of the reported non-HIF substrates using either method. In contrast, control assays with HIF1-alpha substrate supported high stoichiometry (typically >90%) hydroxylation. Our findings suggest that PHD substrates are more restricted than has been reported.

2019-08-30 | PXD013112 | Pride

The RPB2 flap loop of human RNA polymerase II is dispensable for transcription initiation and elongation.

Project description:Deletion of the flap loop in the Rp2 subunit of human RNAPII did not alter the ability of human RNAPII to initiate transcription or elongate the initiated transcripts in vivo and in vitro, and was also dispensable for elongation factor-mediated enhancement and inhibition of transcript elongation in vitro. ChIP:chip of wild-type and flap deletion human RNAPII revealed that the mutant RNAPII was not defective for promoter binding, initiation and elongation in vivo. Eight ChIP datasets were generated as log2(IP/input) fluorescence intensities using anti-FLAG IP of wild-type RPB2-FLAG cells in biological triplicate, anti-FLAG IP of delta-FL RPB2 FLAG cells in biological triplicate, and anti-RPB1 CTD, 8WG16 of both wild-type and delta-FL cells in biological duplicate. The two 8WG16- IP datasets were combined to measure the distribution of RPB1 signal.

2011-06-24 | E-GEOD-29734 | biostudies-arrayexpress

hydroxyproline-containing proteins of rice

Project description:Identification of hydroxyproline-containing proteins and hydroxylation of proline in rice

2020-06-09 | PXD017798 |