ABSTRACT: Caenorhabditis elegans Raw sequence reads-Evaluation of Short-chain Chlorinated Paraffins which can induce germ-cell mutagenesis in alternative in vivo model Caenorhabditis elegans
Project description:Caenorhabditis elegans Raw sequence reads-Evaluation of chemotherapeutic agent oxaliplatin-induced germ-cell mutagenesis in alternative in vivo model Caenorhabditis elegans
Project description:Caenorhabditis elegans Raw sequence reads-Evaluation of chemotherapeutic agent Flame retardant of TBBPA, TCEP, TCPP which can induce germ-cell mutagenesis in alternative in vivo model Caenorhabditis elegans
Project description:Caenorhabditis elegans Raw sequence reads-Evaluation of heavy metal of potassium dichromate, cadmium chloride, sodium arsenite which can induce germ-cell mutagenesis in alternative in vivo model Caenorhabditis elegans
Project description:Raw sequence reads Evaluation of chemotherapeutic agent oxaliplatin-induced germ-cell mutagenesis in alternative in vivo model Caenorhabditis elegans
Project description:Many biomolecular condensates such as stress granules, P bodies, nucleoli, and germ granules contain sub-compartments. For instance, the Caenorhabditis elegans germ granule, which localizes near the outer nuclear membrane of germ cell nuclei, is composed of at least four ordered compartments, each housing distinct sets of proteins and RNAs. How these compartments might form, and why these compartments are ordered in space, remain poorly understood. Here we show that the conserved RNA helicase DDX-19 defines another compartment of the larger Caenorhabditis elegans germ granule, which we name the D compartment. We find that the D compartment exhibits properties of a liquid condensate and that it localizes between the outer nuclear pore filament and other compartments of the germ granule. Two nuclear pore proteins NPP-14 and GLE-1, whose homologs are known to interact with DDX-19 homologs in other eukaryotes, are required for D compartment formation, suggesting that the D compartment localizes adjacent to the outer nuclear membrane via interactions with the nuclear pore. The loss of DDX-19, NPP-14, or GLE-1 leads to; 1) aberrant morphology, assembly, and ordering of the other four germ granule compartments; 2) a loss of germline immortality; and 3) dysregulation of RNA-based transgenerational epigenetic inheritance programs. Hence, we propose that one function of DDX-19 and the D compartment is to help anchor the larger germ granule to nuclear pores, which enables germ granule compartmentalization and empowers transgenerational RNA surveillance.
Project description:The Cell Division Cycle and Apoptosis Regulator (CCAR) protein family members have recently emerged as regulators of alternative splicing and transcription, as well as having other key physiological functions. For example, mammalian CCAR2/DBC1 forms a complex with the zinc factor protein ZNF326 to integrate alternative splicing with RNA polymerase II transcriptional elongation in AT-rich regions of the DNA. Additionally, Caenorhabditis elegans CCAR-1, a homolog to mammalian CCAR2, facilitates the alternative splicing of the perlecan unc-52 gene. However, much about the CCAR family's role in alternative splicing is unknown. We are interested in uncovering the role of the CCAR family in alternative splicing in vivo using Caenorhabditis elegans. We examined the role of CCAR-1 in genome-wide alternative splicing and identified new alternative splicing targets of CCAR-1 using RNA sequencing. Also, we found that CCAR-1 interacts with the spliceosome factors UAF-1 and UAF-2 using mass spectrometry, and that knockdown of ccar-1 affects alternative splicing patterns, motility, and proteostasis of UAF-1 mutant worms. Collectively, we demonstrate a role for CCAR-1 in the regulation of global alternative splicing in C. elegans and in conjunction with UAF-1
Project description:In higher eukaryotes, splicing of introns from pre-mRNAs is required for gene expression. Here, we report that Caenorhabditis elegans MOG-7 is a hybrid RNA splicing factor that contains conserved splicing domains from both yeast and mammals. Acute removal of MOG-7 from the C. elegans germline causes intron retention in the majority of genes, resulting in sterility, germline masculinization and germ cell morphology defects. Despite the deleterious consequences caused by MOG-7 loss, the germline can functionally recover to produce viable and fertile progeny once MOG-7 expression is restored through apoptotic clearance of defective germ cells.
Project description:It has been shown in vitro that only specific dietary-fibers contribute to immunity but studies in vivo are not conclusive. Here we investigated degree of polymerization (DP) dependent effects of β2→1-fructans on immunity via microbiota-dependent and -independent effects. To this end, conventional or germ-free mice received short- or long-chain β2→1-fructan for 5 days. Immune cell populations in the spleen, mesenteric lymph nodes (MLN), and Peyer's patches (PPs) were analyzed with flow cytometry, genome-wide gene expression in the ileum was measured with microarray, and gut microbiota composition was analyzed with 16S rRNA sequencing of fecal samples. We found that β2→1-fructans modulated immunity by both microbiota and microbiota-independent effects. Moreover, effects were dependent on the chain-length of the β2→1-fructans type polymer. Both short- and long-chain β2→1-fructans enhanced T-helper 1 cells in Peyer's patches, whereas only short-chain β2→1-fructans increased regulatory T cells and CD11b-CD103- DCs in the MLN. A common feature after short- and long-chain β2→1-fructan treatment was enhanced Fut2 expression and other IL-22-dependent genes in the ileum of conventional mice. These effects were not associated with shifts in gut microbiota composition, or altered production of short-chain fatty acids. Both short- and long-chain β2→1-fructans also induced immune effects in germ-free animals, demonstrating direct effect independent from the gut microbiota. Also, these effects were dependent on the chain-length of the β2→1-fructans. Short-chain β2→1-fructan induced lower CD80 expression by CD11b-CD103- DCs in PPs, whereas long-chain β2→1-fructan specifically modulated B cell responses in germ-free mice. In conclusion, support of immunity is determined by the chemical structure of β2→1-fructans and is partially microbiota-independent.