Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Multiple mechanisms of global microRNA suppression in vertebrate oocytes

ABSTRACT: Multiple mechanisms of global microRNA suppression in vertebrate oocytes

PROVIDER: PRJNA358569 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR5125820_1.fastq.gz	Fastqsanger.gz
	SRR5125820_2.fastq.gz	Fastqsanger.gz
	SRR5125821_1.fastq.gz	Fastqsanger.gz
	SRR5125821_2.fastq.gz	Fastqsanger.gz
	SRR5125822_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 16

Similar Datasets

Multiple mechanisms of global microRNA suppression in vertebrate oocytes [expression]

Project description:Mouse oocyte maturation, fertilization, and reprogramming occur in the absence of transcription and thus must be regulated post-transcriptionally. Surprisingly, a major form of post-transcriptional regulation, microRNA-based transcript destabilization and translational inhibition, is lost during this developmental window. Here we evaluate the conservation, timing, and mechanism behind the loss of microRNA activity in oocytes. In both mouse and frogs, microRNA function was active in growing oocytes, but then lost during oocyte maturation. RNA-sequencing of the maturing oocytes uncovered expression of an alternative isoform of Ago2 lacking domains critical for its function. Introduction of full-length Ago2 together with an exogenous microRNA destabilized microRNA luciferase reporters. However, endogenous targets were still largely unaffected. These findings suggest that while it is possible to re-activate some aspects of microRNA activity by introducing full length Ago2, there are additional mechanisms to protect endogenous transcripts from microRNA activity in oocytes.

2017-12-31 | GSE92658 | GEO

Multiple mechanisms of global microRNA suppression in vertebrate oocytes [RNA-seq]

2017-12-31 | GSE92761 | GEO

Multiple mechanisms of global microRNA suppression in vertebrate oocytes

Project description:This SuperSeries is composed of the SubSeries listed below.

2017-12-31 | GSE92768 | GEO

Cordycepin Delays Postovulatory Aging of Mammalian Oocytes through Inhibition of Maternal mRNAs Degradation via DCP1A Polyadenylation Suppression

Project description:Postovulatory aging leads to the decline in oocyte quality and subsequent impairment of embryonic development, thereby reducing the success rates of assisted reproductive technology (ART). Nevertheless, potential preventative strategies to improve aging oocytes quality and the associated underlying mechanisms warrant further investigation. In this study, we identify cordycepin, an natural nucleoside analogue, as having the potential to restore the postovulatory aging-induced decline in oocyte quality, including aspects such as oocyte fragmentation, embryonic developmental competence, spindle/chromosomes morphology and mitochondrial function. Proteomic and RNA sequencing analyses revealed that cordycepin inhibited the degradation of several crucial maternal proteins and mRNAs caused by aging. Mechanistically, cordycepin was found to suppress the elevation of DCP1A protein levels by inhibiting polyadenylation during postovulatory aging, consequently impeding the decapping of maternal mRNAs. In humans, the increased degradation of DCP1A and total mRNA during aging was also inhibited by cordycepin. Collectively, our findings demonstrate that cordycepin may prevent postovulatory aging of mammalian oocytes by inhibition of maternal mRNAs degradation via DCP1A polyadenylation suppression, thereby promoting the successful rates of ART procedure.

2024-01-26 | PXD042600 | Pride

Control of poly(A)-tail length and translation in vertebrate oocytes and early embryos

Project description:Control of poly(A)-tail length and translation in vertebrate oocytes and early embryos

| PRJNA1006406 | ENA

Association of maternal mRNA with the spindle in mouse oocytes

Project description:The oocytes of many species, both invertebrate and vertebrate, contain a large collection of localized determinants in the form of proteins and translationally inactive maternal mRNAs. However, it is unknown whether mouse oocytes contain localized MmRNA determinants and what mechanisms might be responsible for their control. We collected intact MII oocytes, enucleated MII oocyte cytoplasts (with the spindle removed), and spindle-chromosome complexes which had been microsurgically removed. RNA was extracted, amplified, labeled, and applied to microarrays to determine if any MmRNA determinants were localized to the SCC. We used microarrays to determine whether maternal mRNAs in mouse oocytes are enriched in the meiotic spindle

2013-11-06 | E-GEOD-46875 | biostudies-arrayexpress

Association of maternal mRNA with the spindle in mouse oocytes

2013-11-06 | GSE46875 | GEO

The global phosphorylation landscape of mouse oocytes during meiotic maturation

Project description:To explore the impact of BTG4-T145/S146/S147 mutations on the degradation of transcripts in MII-stage oocytes, we injected wild-type BTG4 mRNA (BTG4wt) and mutant BTG4 mRNA (BTG4tm) into GV-stage oocytes. These oocytes were matured in vitro to the MII stage, after which samples of MII-stage oocytes were collected for library construction and subsequent second-generation transcriptome sequencing.

2024-10-23 | GSE261544 | GEO

Mus musculus

Project description:Multiple mechanisms of global microRNA suppression in vertebrate oocytes [expression]

| PRJNA358251 | ENA

The translation regulator Zar1l is required to control the timing of meiosis in Xenopus oocytes

Project description:In vertebrates, sexual reproduction depends on the precisely temporally controlled translation of mRNAs stockpiled in the oocyte. The RNA-binding proteins Zar1 and Zar2 have been implicated in translational control in oocytes of several vertebrate species, but how they act mechanistically is still incompletely understood. Here, we investigate the function of Zar1l, a so far uncharacterized member of the Zar protein family, in Xenopus laevis oocytes. By combining biochemical assays and mass spectrometry, we reveal that Zar1l is a constituent of a known large ribonucleoparticle containing the translation repressor 4E-T and the central polyadenylation regulator CPEB1. Employing TRIM-Away, we show that depletion of Zar1l from prophase-I arrested oocytes results in premature meiotic maturation upon hormone treatment. We provide evidence that this is based on the precocious expression of the kinase cMos, a key promotor of meiotic resumption. Based on our data, we propose a model according to which degradation of Zar1l results in dissociation of 4E-T from CPEB1, thus weakening translation inhibition imposed by the mRNA 3’UTR of cMos and probably also other M-phase promoting regulators. Thus, our detailed characterization of the function of Zar1l reveals novel mechanistic insights into the regulation of maternal mRNA translation during vertebrate meiosis.

2022-09-22 | PXD032170 | Pride

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