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Mammalian oocytes store mRNAs in a mitochondria-associated membraneless compartment

ABSTRACT: Mammalian oocytes store mRNAs in a mitochondria-associated membraneless compartment

PROVIDER: PRJNA880587 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR21570391_1.fastq.gz	Fastqsanger.gz
	SRR21570391_2.fastq.gz	Fastqsanger.gz
	SRR21570392_1.fastq.gz	Fastqsanger.gz
	SRR21570392_2.fastq.gz	Fastqsanger.gz
	SRR21570393_1.fastq.gz	Fastqsanger.gz

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Mammalian oocytes store mRNAs in a mitochondria-associated membraneless compartment

Project description:Fully-grown oocytes are transcriptionally silent and must stably maintain mRNAs needed for oocyte meiotic maturation and early embryonic development. However, where and how mammalian oocytes store maternal mRNAs is unclear. Here, we report that mammalian oocytes accumulate mRNAs in a mitochondria-associated ribonucleoprotein domain (MARDO). MARDO assembly around mitochondria was promoted by the RNA-binding protein ZAR1, and directed by an increase in mitochondrial membrane potential during oocyte growth. MARDO foci coalesced into hydrogel-like matrices that clustered mitochondria. Maternal mRNAs stored in the MARDO were translationally repressed. Loss of ZAR1 disrupted the MARDO, dispersed mitochondria, and caused a premature loss of MARDO-localized mRNAs. Thus, a mitochondria-associated membraneless compartment controls mitochondrial distribution and regulates maternal mRNA storage, translation and decay to ensure fertility in mammals.

2022-10-25 | PXD036974 | Pride

Mammalian oocytes store mRNAs in a mitochondria-associated membraneless compartment

Project description:To investigate the transcriptomic profile of Zar1 -/- oocytes

2022-10-21 | GSE213351 | GEO

Mammalian oocytes store proteins in cytoplasmic lattices

Project description:Oocytes must accumulate and store maternal factors such as proteins during growth to sustain the first stages of embryonic development. How mammalian oocytes store maternal proteins is not understood. Here, we show that mouse and human oocytes store proteins on cytoplasmic lattices. With super-resolution light microscopy and electron tomography, we demonstrate that cytoplasmic lattices are twisted filament bundles formed by proteins of the subcortical maternal complex, filling the entire ooplasm. The lattices were associated with many proteins that have crucial functions during early embryo development, including proteins controlling genome methylation. Loss of cytoplasmic lattices prevented the accumulation of these proteins and resulted in early embryonic arrest. Thus, cytoplasmic lattices are important for storage of essential maternal proteins and the developmental success of early mammalian embryos.

2023-10-23 | PXD038575 | Pride

Mammalian oocytes store proteins in cytoplasmic lattices

Project description:Mammalian oocytes store proteins in cytoplasmic lattices

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Mammalian oocytes store proteins in cytoplasmic lattices

Project description:To investigate the transcriptomic profile of Padi6 -/- and Tle6 -/- oocytes

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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

LC-MS of control vs BafA1-treated mouse oocytes during maturation

Project description:We discovered that mouse oocytes contain novel non-membrane-bound organelles, which we named EndoLysosomal Vesicular Assemblies (ELVAs). ELVAs contain endolysosomal and autophagy vesicles, as well as proteasomes. In immature oocytes, ELVAs store ubiquitinated proteins and show little degradative activity. During oocyte maturation, ELVAs increase protein degradation, thereby degrading the stored proteins. To understand which proteins are being degraded inside ELVAs during oocyte maturation we treated mouse oocytes with or without the lysosomal inhibitor Bafilomycin A1 (BafA1) during maturation and subjected equal number of in vitro matured oocytes to mass spec, looking for enriched proteins in the BafA1-treated sample.

2024-02-20 | PXD042769 | Pride

Impact of maternal age and in vitro maturation on the transcriptome of denuded human oocytes

Project description:While the oocytes’ transcriptome is predominantly determined by maturation stage, transcripts related to specific pathways such as chromosome segregation, mitochondria and RNA processing are affected by age after in vitro maturation of denuded oocytes.

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The maintenance of oocytes in the mammalian ovary involves extreme protein longevity

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2023-07-26 | MSV000092528 | MassIVE

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

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