Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Overlapping and distinct functions of CstF64 and CstF64τ in mammalian mRNA 3’ processing

ABSTRACT: Overlapping and distinct functions of CstF64 and CstF64τ in mammalian mRNA 3’ processing

PROVIDER: PRJNA221564 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR1002953.fastq.gz	Fastqsanger.gz
	SRR1002954.fastq.gz	Fastqsanger.gz
	SRR1002955.fastq.gz	Fastqsanger.gz
	SRR1002956.fastq.gz	Fastqsanger.gz
	SRR1002957.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 5

Similar Datasets

Overlapping and distinct functions of CstF64 and CstF64τ in mammalian mRNA 3’ processing

Project description:Our study of CstF64 and CstF64τ revealed both functional overlap and specificity of these two important mRNA 3’ processing factors and provided new insights into the regulatory mechanisms of mRNA 3’ processing. CstF64tau iCLIP-seq in HeLa cells; direct RNA sequencing (DRS) of control HeLa cells, CstF64tau-RNAi cells and SELEX-seq for RNA control pool, CstF64 and CstF64tau.

2013-09-30 | E-GEOD-51156 | biostudies-arrayexpress

Overlapping and distinct functions of CstF64 and CstF64τ in mammalian mRNA 3’ processing

2013-09-30 | GSE51156 | GEO

Overlapping and distinct functions of CstF64 and CstF64? in mammalian mRNA 3' processing.

Project description:mRNA 3' processing is dynamically regulated spatially and temporally. However, the underlying mechanisms remain poorly understood. CstF64? is a paralog of the general mRNA 3' processing factor, CstF64, and has been implicated in mediating testis-specific mRNA alternative polyadenylation (APA). However, the functions of CstF64? in mRNA 3' processing have not been systematically investigated. We carried out a comprehensive characterization of CstF64? and compared its properties to those of CstF64. In contrast to previous reports, we found that both CstF64 and CstF64? are widely expressed in mammalian tissues, and their protein levels display tissue-specific variations. We further demonstrated that CstF64 and CstF64? have highly similar RNA-binding specificities both in vitro and in vivo. CstF64 and CstF64? modulate one another's expression and play overlapping as well as distinct roles in regulating global APA profiles. Interestingly, protein interactome analyses revealed key differences between CstF64 and CstF64?, including their interactions with another mRNA 3' processing factor, symplekin. Together, our study of CstF64 and CstF64? revealed both functional overlap and specificity of these two important mRNA 3' processing factors and provided new insights into the regulatory mechanisms of mRNA 3' processing.

| S-EPMC3884657 | biostudies-literature

Overlapping peri-implantation phenotypes of ZNHIT1 and ZNHIT2 despite distinct functions during early mouse development.

Project description:Overlapping peri-implantation phenotypes of ZNHIT1 and ZNHIT2 despite distinct functions during early mouse development.

| PRJNA1157720 | ENA

Overlapping peri-implantation phenotypes of ZNHIT1 and ZNHIT2 despite distinct functions during early mouse development.

Project description:Mammalian preimplantation development culminates in the formation of a blastocyst which undergoes extensive gene expression regulation to successfully implant into the maternal endometrium. Zinc-finger HIT domain-containing (ZNHIT) 1 and 2 are members of a highly conserved family, yet they have been identified as subunits of distinct complexes. Here we report that knockout of either Znhit1 or Znhit2 results in embryonic lethality during peri-implantation stages. Znhit1 and Znhit2 mutant embryos have overlapping phenotypes, including reduced proportion of SOX2-positive ICM cells, a lack of Fgf4 expression and aberrant expression of NANOG and SOX17. Furthermore, we find that the similar phenotypes are caused by distinct mechanisms. Specifically, embryos lacking ZNHIT1 likely fail to incorporate sufficient H2A.Z at the promoter region of Fgf4 and other genes involved in cell projection organization resulting in impaired invasion of trophoblast cells during implantation. In contrast, Znhit2 mutant embryos display a complete lack of nuclear EFTUD2, a key component of U5 spliceosome, indicating a global splicing deficiency. Our findings unveil the indispensable yet distinct roles of ZNHIT1 and ZNHIT2 in early mammalian embryonic development.

2025-09-08 | GSE276496 | GEO

Protein sequence editing defines distinct and overlapping functions of SKN-1A/Nrf1 and SKN-1C/Nrf2.

Project description:Protein sequence editing defines distinct and overlapping functions of SKN-1A/Nrf1 and SKN-1C/Nrf2.

| PRJNA1170320 | ENA

Overlapping and distinct functions between ERα and ERβ homodimers and corresponding transcriptomes in the same cellular context

Project description:Overlapping and distinct functions between ERα and ERβ homodimers and corresponding transcriptomes in the same cellular context

| PRJNA756260 | ENA

Regulons and protein–protein interactions of PRD-containing Bacillus anthracis virulence regulators reveal overlapping but distinct functions

Project description:Regulons and protein–protein interactions of PRD-containing Bacillus anthracis virulence regulators reveal overlapping but distinct functions

| PRJNA639101 | ENA

Protein sequence editing defines distinct and overlapping functions of SKN-1A/Nrf1 and SKN-1C/Nrf2.

Project description:Nrf/NFE2L family transcription factors regulate redox balance, metabolism, proteostasis, and aging. Nrf1/NFE2L1 is responsible for stress-responsive upregulation of proteasome subunit genes and is essential for adaptation to proteotoxic stress. The closely related Nrf2/NFE2L2 is responsible for activation of oxidative stress responses and xenobiotic detoxification. Although regulated by different mechanisms, Nrf1 and Nrf2 contain very similar DNA binding domains and can drive similar transcriptional responses. However, the extent to which functions of Nrf1/2 are distinct or overlapping has been unclear. In C. elegans, a single gene, skn-1, encodes distinct protein isoforms, SKN-1A and SKN-1C, that function analogously to mammalian Nrf1 and Nrf2, respectively. We previously showed that regulation of the proteasome by SKN-1A/Nrf1 requires post-translational conversion of N-glycosylated asparagine residues to aspartate by the PNG-1/NGLY1 peptide:N-glycanase, a process we term ‘sequence editing’. Here, we reveal the consequences of sequence editing for the transcriptomic output of activated SKN-1A. We show that whilst activation of proteasome subunit genes is strictly dependent on sequence editing, sequence edited SKN-1A also activate genes linked to redox homeostasis and xenobiotic detoxification that are also activated by non-sequence edited forms of SKN-1. Using mutant alleles that selectively inactivate either SKN-1A or SKN-1C, we show that SKN-1A/Nrf1 and SKN-1C/Nrf2 function coordinately to promote optimal oxidative stress resistance and confirm that they are regulated by discrete genetic pathways. This work demonstrates that sequence editing plays a critical role in tailoring SKN-1/Nrf functions by tuning the SKN-1A/Nrf1 regulated transcriptome.

2025-06-17 | GSE279082 | GEO

High-throughput differentiation of human blood vessel organoids reveals overlapping and distinct functions of the cerebral cavernous malformation proteins

Project description:High-throughput differentiation of human blood vessel organoids reveals overlapping and distinct functions of the cerebral cavernous malformation proteins

| PRJNA1157719 | ENA

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