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CLIP of mRNA capping enzyme CMTR1 in Drosophila melanogaster

ABSTRACT: CLIP of mRNA capping enzyme CMTR1 in Drosophila melanogaster

PROVIDER: PRJNA751571 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR15324531_1.fastq.gz	Fastqsanger.gz
	SRR15324531_2.fastq.gz	Fastqsanger.gz
	SRR15324532_1.fastq.gz	Fastqsanger.gz
	SRR15324532_2.fastq.gz	Fastqsanger.gz
	SRR15324533_1.fastq.gz	Fastqsanger.gz

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CLIP of mRNA capping enzyme CMTR1 in Drosophila melanogaster

Project description:The mRNA cap structure consists of the m7G "cap0" linked to the 5'-most nucleotide of the initial mRNA. The first two nucleotides of mRNA can be 2'-O-Ribose modified to form cap1 or cap2 structures. Here, mRNA was sequenced after CLIP with tagged recombinant CMTR1 and compared to input RNA.

2021-12-18 | GSE181321 | GEO

CLIP of mRNA capping enzyme CMTR2 in drosophila melanogaster

Project description:CLIP of mRNA capping enzyme CMTR2 in drosophila melanogaster

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CLIP of mRNA capping enzyme CMTR2 in drosophila melanogaster

2021-12-18 | GSE138868 | GEO

Identification of re-capping substrates for the cytoplasmic capping enzyme complex

Project description:The analysis of capped RNAs by massively parallel sequencing has identified a large number of previously unknown transcripts, some of which are small RNAs and others are 5M-bM-^@M-^Y truncated forms of RefSeq genes. The latter may be generated by endonuclease cleavage or by stalling of Xrn1 at defined sites. With the exception of promoter-proximal transcripts the caps on all of these are added post-transcriptionally by a cytoplasmic capping enzyme complex that includes capping enzyme and a kinase that converts 5M-bM-^@M-^Y-monophosphate ends to a diphosphate capping substrate. We previously described a modified form of capping enzyme with dominant negative activity against cytoplasmic capping (DN-cCE). A tet-inducible form of this was used to identify substrates for cytoplasmic capping by treating cytoplasmic RNA from control and induced cells with and without Xrn1. Surviving RNA was analyzed on Affymetrix Human Exon 1.0 arrays and scored for changes in probe intensity as a function of its position on each RefSeq gene to derive a factor (alpha) that could be compared between sets. Notably, transcriptome-wide changes were not evident unless RNA was treated with Xrn1. This analysis identified 2,666 uncapped mRNAs in uninduced cells, 672 mRNAs that appeared in the uncapped pool in cells expressing DN-cCE, and 835 mRNAs that were in both populations. Changes in cap status of 10 re-capping targets and 5 controls were assessed by 3 independent measures; susceptibility to Xrn1, recovery with a biotin-tagged DNA primer after ligating a complementary RNA oligonucleotide to uncapped 5M-bM-^@M-^Y ends, and binding or exclusion from a high affinity cap-binding matrix comprised of immobilized eIF4E and the corresponding binding domain of eIF4G. 3 biological replicates of 4 different samples comparing XRN1 treatment/non-treatment and Dox induction/non-induction of K294A

2012-12-20 | E-GEOD-36729 | biostudies-arrayexpress

Identification of re-capping substrates for the cytoplasmic capping enzyme complex

Project description:The analysis of capped RNAs by massively parallel sequencing has identified a large number of previously unknown transcripts, some of which are small RNAs and others are 5’ truncated forms of RefSeq genes. The latter may be generated by endonuclease cleavage or by stalling of Xrn1 at defined sites. With the exception of promoter-proximal transcripts the caps on all of these are added post-transcriptionally by a cytoplasmic capping enzyme complex that includes capping enzyme and a kinase that converts 5’-monophosphate ends to a diphosphate capping substrate. We previously described a modified form of capping enzyme with dominant negative activity against cytoplasmic capping (DN-cCE). A tet-inducible form of this was used to identify substrates for cytoplasmic capping by treating cytoplasmic RNA from control and induced cells with and without Xrn1. Surviving RNA was analyzed on Affymetrix Human Exon 1.0 arrays and scored for changes in probe intensity as a function of its position on each RefSeq gene to derive a factor (alpha) that could be compared between sets. Notably, transcriptome-wide changes were not evident unless RNA was treated with Xrn1. This analysis identified 2,666 uncapped mRNAs in uninduced cells, 672 mRNAs that appeared in the uncapped pool in cells expressing DN-cCE, and 835 mRNAs that were in both populations. Changes in cap status of 10 re-capping targets and 5 controls were assessed by 3 independent measures; susceptibility to Xrn1, recovery with a biotin-tagged DNA primer after ligating a complementary RNA oligonucleotide to uncapped 5’ ends, and binding or exclusion from a high affinity cap-binding matrix comprised of immobilized eIF4E and the corresponding binding domain of eIF4G.

2012-12-20 | GSE36729 | GEO

Cytoplasmic capping enzyme interactome

Project description:Formaldehyde crosslinking and Proximity-dependent biotinylation methods were applied to study the cytoplasmic capping enzyme interactome via 1D-LC-MS/MS. The raw data were searched against Uniprot human database modified to contain our designed protein sequences using the Thermo Proteome Discoverer software (v 1.4.1.14).

2018-08-30 | PXD010368 | JPOST Repository

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2023-09-30 | E-MTAB-2235 | biostudies-arrayexpress

CK2 phosphorylation of cap methyltransferase CMTR1 promotes RNAPII interaction

Project description:We investigated influence of CMTR1 phosphorylation by CK2 on RNA expression. In this experiment, we added wild-type and phosphorylation deficient mutant of CMTR1 and knocked out the endogenous CMTR1. We demonstrated that lack of phosphorylation of CMTR1 affects only small but specific group of genes.

2024-06-24 | GSE200103 | GEO

DHX15 regulates CMTR1-dependent gene expression and cell proliferation

Project description:We discovered that the RNA helicase DHX15 is a regulator of the methyltransferase CMTR1. To determine the biological consequences of this interaction we overexpressed CMTR1 or a mutated CMTR1 (2LA)that does not bind DHX15, in the human breast cancer cell line HCC1806. To assess the effects of the DHX15-CMTR1 interaction on translation, polysomes were separated on a sucrose gradient and sequencing libraries generated from the polysomal and input RNA. We found that the DHX15-CMTR1 interaction controls ribosome loading of a subset of mRNAs and impacts on cell proliferation.

2018-06-05 | GSE113573 | GEO

METTL3 alters capping enzyme expression and its activity on ribosomal proteins in NSCLC cell model

Project description:The 5’ cap, catalyzed by capping enzyme, RNGTT, is a vital mRNA modification for the functionality of mRNAs and dysregulated in cancer cells. The m6A writer METTL3 is a regulator of mRNA stability and protein translation, and its expression is altered in various cancers, including lung cancer cells. We identified a METTL3 motif in the mRNA of RNGTT and investigated whether METTL3 could regulate the expression of RNGTT. Knock down of METTL3 resulted in destabilizing RNGTT mRNA, reduced protein expression and activity. Sequencing of capped mRNAs and m7G immunoprecipitation identified an underrepresentation of ribosomal protein mRNA.

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