Caenorhabditis elegans
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA251377 | ENA |
REPOSITORIES: ENA
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Project description:A novel small molecule that disrupts the oocyte-to-embryo transition in C. elegans
| PRJNA329115 | ENA
Project description:LIN-41 and OMA ribonucleoprotein complexes mediate a translational repression-to-activation switch controlling oocyte meiotic maturation and the oocyte-to-embryo transition in Caenorhabditis elegans
| PRJNA384040 | ENA
Project description:During oocyte maturation and the oocyte-to-embryo transition, key developmental regulators such as RNA-binding proteins coordinate translation of particular mRNAs and related developmental processes by binding to their cognate maternal mRNAs. In the nematode C. elegans, these processes are regulated by a set of CCCH zinc finger proteins. OMA-1 and OMA-2 are two functionally redundant CCCH zinc finger proteins that turnover rapidly during the first embryonic cell division. These turnovers are required for proper transition from oogenesis to embryogenesis. A gain-of-function mutant of OMA-1, oma-1(zu405), stabilizes and delays degradation of OMA-1, resulting in delayed turnover and mis-segregation of other cell fate determinants, which eventually causes embryonic lethality. We performed a large-scale forward genetic screen to identify suppressors of the oma-1(zu405) mutant. We show here that multiple alleles affecting functions of various APC/C subunits, including MAT-1, MAT-2, MAT-3, EMB-30, and FZY-1, suppress the gain-of-function mutant of OMA-1. Mutations in APC/C genes prevent OMA-1 enrichment in P granules and correct delayed degradation of downstream cell fate determinants including PIE-1, POS-1, MEX-3, and MEG-1. Transcriptome analysis also suggested that overall transcription in early embryos occurred after introducing mutations in APC/C genes into the oma-1(zu405) mutant. We demonstrated that only the activator FZY-1, but not FZR-1, is incorporated in the APC/C complex to regulate the oocyte-to-embryo transition. Our findings suggested a genetic relationship linking the APC/C complex and OMA-1, and support a model in which the APC/C complex promotes P granule accumulation and modifies RNA binding of OMA-1 to regulate the oocyte-to-embryo transition process.
2021-10-02 | GSE181115 | GEO
Project description:C elegans N2 Late embryo input control
| PRJNA148537 | ENA
Project description:Global analysis of Caenorhabditis elegans operons
| PRJNA91921 | ENA
Project description:To elucidate the molecular mechanism underlying lifespan reduction induced by PM2.5 exposure in Caenorhabditis elegans, we performed global gene expression profiling by RNA-sequencing technology, and compared the gene expression pattern change induced by PM2.5 exposure.
2023-02-22 | GSE214215 | GEO
Project description:The gastrula transition reorganizes replication origin selection in Caenorhabditis elegans
| PRJNA342483 | ENA
Project description:Global analysis of dauer gene expression in Caenorhabditis elegans
| PRJNA92707 | ENA
Project description:Global profile of germline gene expression in C. elegans
| PRJNA85207 | ENA
Project description:The complex cellular events that occur in response to fertilization are essential for mediating the oocyte-to-embryo transition. Here, we describe a comprehensive small molecule screen focused on identifying compounds that affect the oocyte-to-embryo transition in C. elegans. We identify a single novel compound that disrupts early embryogenesis with remarkable stage- and species-specificity. The compound, named C22, primarily impairs eggshell integrity, leading to osmotic sensitivity and embryonic lethality. We show that this phenotype is dependent upon the upregulation of the LET-607/CREBH transcription factor. We then demonstrate that LET-607 candidate gene targets primarily encode factors involved in diverse aspects of protein trafficking. Together, our data suggest that in the presence of C22, one or more key components of the eggshell are inappropriately processed, leading to permeable, inviable embryos. The remarkable specificity and reversibility of this compound will facilitate further investigation into the role and regulation of protein trafficking in the early embryo, as well as serve as a tool for manipulating the life cycle for other studies such as aging.
2016-12-06 | GSE84419 | GEO