Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

To investigate gene expression changes in neurons lacking cap methyltransferase 1 (CMTR1)

ABSTRACT: To investigate gene expression changes in neurons lacking cap methyltransferase 1 (CMTR1)

PROVIDER: PRJNA606450 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Similar Datasets

To investigate gene expression changes in neurons lacking cap methyltransferase 1 (CMTR1)

Project description:Transcriptomic profiles of control and CMTR1-knockdown neurons.

2020-09-25 | GSE145223 | GEO

CK2 phosphorylation of cap methyltransferase CMTR1 promotes RNAPII interaction

Project description:CK2 phosphorylation of cap methyltransferase CMTR1 promotes RNAPII interaction

| PRJNA823002 | ENA

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

CMTR1 is recruited to transcription start sites and has enhanced influence over ribosomal protein and histone genes [RNA-seq]

Project description:We investigated the gene-specificity of mRNA cap methyltransferase CMTR1 and its impact in RNA expression. In this RNA-seq experiment, we used siRNA to knockdown the endogenous CMTR1 protein to investigate its role in mouse embryonic stem cells. We demonstrated that the repression of CMTR1 expression resulted in a loss of RNA expression, particularly of histone and ribosomal protein genes.

2022-02-25 | GSE175629 | GEO

CMTR1 is recruited to transcription start sites and has enhanced influence over ribosomal protein and histone genes [ChIP-seq]

Project description:We investigated the gene-specificity of mRNA cap methyltransferase CMTR1 and its impact in RNA expression. In this ChIP-seq experiment, we investigated the genome-wide chromatin binding profiles of CMTR1 in mouse embryonic stem cells. We demontrated that CMTR1 binds to the transcription start site (TSS) correlating with RNA polymerase II (RNAP II) levels, with predominant binding at histone genes and ribosomal protein (RP) genes. Moreover, the repression of CMTR1 expression resulted in a loss of RNAP II binding at the TSS.

2022-02-25 | GSE175628 | 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

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

2'-O-methylation of the second transcribed nucleotide in eukaryotic RNA 5’ cap impacts protein production levels and susceptibility to DXO-mediated transcript degradation

Project description:Eukaryotic mRNA 5’ end is decorated with cap structure which plays multiple roles in the cell. Most importantly, protects transcript from exonucleolytic degradation and enables translation of encoded protein conducted by cap-dependent machinery. This is also a key feature in the process of recognizing RNA as self or non-self molecule by cellular innate immune system. Cap is composed of 7-methylguanosine linked by a 5′,5′-triphosphate chain to the first transcribed nucleotide, and is formed enzymatically during transcription. This m7GpppN structure, called cap0, can be further modified by CMTR1 methyltransferase to cap1 (m7GpppNm), which predominates in eukaryotic cells. Cap2, with additional 2′-O-methylation at the second transcribed nucleotide (m7GpppNmpNm) added by another methyltransferase CMTR2, also can be found at mRNA 5’ end. We present new tools allowing for in vitro synthesis of RNAs possessing cap2, i.e tetranucleotide cap analogues. Utilizing these for in vitro transcription reactions we obtained RNAs with 2′-O-methylation present at the second transcribed nucleotide. Due to that we investigated the role of cap2 in protein production from reporter mRNA protected with this structure in different conditions, normal or stress ones, or with CMTR1/2 down regulated level. We also assessed the affinity of eIF4E protein to differentially capped RNAs. Furthermore, we verified whether an additional 2′-O-methylation presence in capped RNA makes transcript more resistant to decapping enzyme action.

2022-09-08 | PXD028636 | Pride

Part 2 JAWS; 2'-O-methylation of the second transcribed nucleotide in eukaryotic RNA 5’ cap impacts protein production levels and susceptibility to DXO-mediated transcript degradation

2022-09-08 | PXD028635 | Pride

mRNA cap methyltransferase, RNMT-RAM, promotes RNA pol II transcription

Project description:mRNA cap addition occurs early during RNA pol II transcription, facilitating pre-mRNA processing and translation. We report that the mammalian mRNA cap methyltransferase, RNMT-RAM, promotes RNA pol II transcription, independently of mRNA capping and translation. In cells, sub-lethal suppression of RNMT-RAM reduces RNA pol II occupancy, net mRNA synthesis and pre-mRNA levels. Conversely, expression of RNMT-RAM increases transcription independently of cap methyltransferase activity. In isolated nuclei, recombinant RNMT-RAM stimulates transcriptional output; this requires the RAM RNA-binding domain. RNMT-RAM interacts with nascent transcripts along their entire length and with transcription associated factors including RNA pol II subunits, SPT4, SPT6 and PAFc. Suppression of RNMT-RAM inhibits transcriptional markers including histone H2B K120 ubiquitination, H3 K4 and K36 methylation, RNA pol II S5 and S2 phosphorylation and PAFc recruitment. These findings suggest that multiple interactions between RNMT-RAM, RNA pol II factors and RNA along the transcription unit stimulate transcription.

2018-05-01 | GSE87767 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data