scholarly journals New genetic regulators question relevance of abundant yolk protein production in C. elegans

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Liesbeth Van Rompay ◽  
Charline Borghgraef ◽  
Isabel Beets ◽  
Jelle Caers ◽  
Liesbet Temmerman
Keyword(s):  
Protein Production ◽  
Yolk Protein ◽  
C Elegans

Similarity of DNA binding and transcriptional regulation by Caenorhabditis elegans MAB-3 and Drosophila melanogaster DSX suggests conservation of sex determining mechanisms

Development ◽  
1999 ◽  
Vol 126 (5) ◽  
pp. 873-881 ◽  
Author(s):  
W. Yi ◽  
D. Zarkower
Keyword(s):  
Dna Binding ◽  
Sex Determination ◽  
Dna Sequences ◽  
Sexual Development ◽  
Yolk Protein ◽  
Binding Motif ◽  
C Elegans ◽  
A Site

Although most animals occur in two sexes, the molecular pathways they employ to control sexual development vary considerably. The only known molecular similarity between phyla in sex determination is between two genes, mab-3 from C. elegans, and doublesex (dsx) from Drosophila. Both genes contain a DNA binding motif called a DM domain and they regulate similar aspects of sexual development, including yolk protein synthesis and peripheral nervous system differentiation. Here we show that MAB-3, like the DSX proteins, is a direct regulator of yolk protein gene transcription. We show that despite containing different numbers of DM domains MAB-3 and DSX bind to similar DNA sequences. mab-3 mutations deregulate vitellogenin synthesis at the level of transcription, resulting in expression in both sexes, and the vitellogenin genes have potential MAB-3 binding sites upstream of their transcriptional start sites. MAB-3 binds to a site in the vit-2 promoter in vitro, and this site is required in vivo to prevent transcription of a vit-2 reporter construct in males, suggesting that MAB-3 is a direct repressor of vitellogenin transcription. This is the first direct link between the sex determination regulatory pathway and sex-specific structural genes in C. elegans, and it suggests that nematodes and insects use at least some of the same mechanisms to control sexual development.

scholarly journals Characterization of RNA binding proteins required for receptor-mediated endocytosis in C. elegans

2019 ◽  
Vol 2 (1) ◽  
Author(s):  
Margaret D. Holdeman ◽  
Farida Daouda ◽  
Heather A. Hundley, Ph.D.
Keyword(s):  
Oocyte Maturation ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Model Organism ◽  
Yolk Protein ◽  
Fluorescent Intensity ◽  
Knock Out ◽  
Receptor Mediated Endocytosis ◽  
C Elegans

Background and Hypothesis: Recently, a study conducted by the Hundley lab revealed that mutation of a specific RNA editing protein, ADR2, in the model organism C. elegans increased receptor-mediated endocytosis of yolk protein vit-2 and oocyte maturation. Of interest to us was what additional RNA binding proteins were involved in the expression of vit-2. To this end, RNA interference (RNAi) was used to knock out relevant RNA binding proteins. We hypothesized we would find candidates that both enhanced and reduced the expression of vit-2. Project Methods: Previously, adr-2(-) C. elegans strain expressing a yolk protein (vit-2) fused to GFP and a library of E. coli strains expressing RNAi directed to specific RNA binding proteins were engineered. vit-2:GFP reporter worms were grown on each RNAi bacterial strain. The COPAS Biosort, a large particle sorter which detects fluorescent intensity, was used to visualize and quantify vit-2 endocytosis. Results: Our screen yielded ten candidate proteins. These proteins had various functions and were expressed in different tissues, most commonly the nervous and reproductive systems. Remarkably, proteins gld-1 and puf-8 are negative regulators of oocyte fate determination and spermatogenesis respectively. Unlike the rest of our candidates, mutation of these two proteins did not have an observed effect on developmental progression but still caused significant increase in vit-2 expression. Conclusion and Potential Impact: This screen successfully gave direction to future studies of ADR-2 involvement in yolk protein uptake, oocyte maturation, and embryonic development. Two of our identified targets seem to be involved in reproductive processes. The remainder may be affecting vit-2 expression by altering development or receptor-mediated endocytosis. Our goal in the immediate future will be to compare loss of these target proteins in wildtype worms to loss in adr-2(-) worms. This would add to what is known about ADARs and life span and possibly demonstrate a role for ADARs in germ cell maturation.  

The glycomes of Caenorhabditis elegans and other model organisms

2002 ◽  
Vol 69 ◽  
pp. 117-134 ◽  
Author(s):  
Stuart M. Haslam ◽  
David Gems ◽  
Howard R. Morris ◽  
Anne Dell
Keyword(s):  
Caenorhabditis Elegans ◽  
Current Knowledge ◽  
Structural Data ◽  
Model Organisms ◽  
Entire Genome ◽  
C Elegans ◽  
The Face ◽  
Area Of Concern ◽  
Nematode Worm

There is no doubt that the immense amount of information that is being generated by the initial sequencing and secondary interrogation of various genomes will change the face of glycobiological research. However, a major area of concern is that detailed structural knowledge of the ultimate products of genes that are identified as being involved in glycoconjugate biosynthesis is still limited. This is illustrated clearly by the nematode worm Caenorhabditis elegans, which was the first multicellular organism to have its entire genome sequenced. To date, only limited structural data on the glycosylated molecules of this organism have been reported. Our laboratory is addressing this problem by performing detailed MS structural characterization of the N-linked glycans of C. elegans; high-mannose structures dominate, with only minor amounts of complex-type structures. Novel, highly fucosylated truncated structures are also present which are difucosylated on the proximal N-acetylglucosamine of the chitobiose core as well as containing unusual Fucα1–2Gal1–2Man as peripheral structures. The implications of these results in terms of the identification of ligands for genomically predicted lectins and potential glycosyltransferases are discussed in this chapter. Current knowledge on the glycomes of other model organisms such as Dictyostelium discoideum, Saccharomyces cerevisiae and Drosophila melanogaster is also discussed briefly.

How do histone modifications contribute to transgenerational epigenetic inheritance in C. elegans?

2020 ◽  
Vol 48 (3) ◽  
pp. 1019-1034 ◽  
Author(s):  
Rachel M. Woodhouse ◽  
Alyson Ashe
Keyword(s):  
Histone Modifications ◽  
Molecular Mechanisms ◽  
Epigenetic Inheritance ◽  
Nematode Caenorhabditis Elegans ◽  
Histone Methyltransferases ◽  
Transgenerational Epigenetic Inheritance ◽  
C Elegans ◽  
Recent Developments ◽  
Gene Regulatory

Gene regulatory information can be inherited between generations in a phenomenon termed transgenerational epigenetic inheritance (TEI). While examples of TEI in many animals accumulate, the nematode Caenorhabditis elegans has proven particularly useful in investigating the underlying molecular mechanisms of this phenomenon. In C. elegans and other animals, the modification of histone proteins has emerged as a potential carrier and effector of transgenerational epigenetic information. In this review, we explore the contribution of histone modifications to TEI in C. elegans. We describe the role of repressive histone marks, histone methyltransferases, and associated chromatin factors in heritable gene silencing, and discuss recent developments and unanswered questions in how these factors integrate with other known TEI mechanisms. We also review the transgenerational effects of the manipulation of histone modifications on germline health and longevity.

Centrosome Aurora A gradient ensures single polarity axis in C. elegans embryos

2020 ◽  
Vol 48 (3) ◽  
pp. 1243-1253 ◽  
Author(s):  
Sukriti Kapoor ◽  
Sachin Kotak
Keyword(s):  
Symmetry Breaking ◽  
Cell Fate ◽  
Cell Cortex ◽  
Axis Formation ◽  
Aurora A Kinase ◽  
Aurora A ◽  
C Elegans ◽  
Cell Embryo ◽  
Polarity Establishment

Cellular asymmetries are vital for generating cell fate diversity during development and in stem cells. In the newly fertilized Caenorhabditis elegans embryo, centrosomes are responsible for polarity establishment, i.e. anterior–posterior body axis formation. The signal for polarity originates from the centrosomes and is transmitted to the cell cortex, where it disassembles the actomyosin network. This event leads to symmetry breaking and the establishment of distinct domains of evolutionarily conserved PAR proteins. However, the identity of an essential component that localizes to the centrosomes and promotes symmetry breaking was unknown. Recent work has uncovered that the loss of Aurora A kinase (AIR-1 in C. elegans and hereafter referred to as Aurora A) in the one-cell embryo disrupts stereotypical actomyosin-based cortical flows that occur at the time of polarity establishment. This misregulation of actomyosin flow dynamics results in the occurrence of two polarity axes. Notably, the role of Aurora A in ensuring a single polarity axis is independent of its well-established function in centrosome maturation. The mechanism by which Aurora A directs symmetry breaking is likely through direct regulation of Rho-dependent contractility. In this mini-review, we will discuss the unconventional role of Aurora A kinase in polarity establishment in C. elegans embryos and propose a refined model of centrosome-dependent symmetry breaking.

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