Katschinski DM et al. (2003) Physiol Genomics "Hot worms can handle heavy metal. Focus on "HIF-1 is required for heat acclimation in the nematode Caenorhabditis elegans"."

Glueck SB, Katschinski DM

[Physiol Genomics, 2003]

Life developed in a stressful environment. Stressors at the cellular level include heat, hypoxia, oxidative or reductive substances, mechanical or osmotic pressure, and toxic compounds like heavy metals. Various molecular pathways, more or less specific for the different stressors, developed during evolution to combat the molecular consequences of cell stress. Thermal stress induces the induction of a highly conserved protein family, the heat shock proteins (HSP).

Gan WJ et al. (2020) Front Cell Dev Biol "Mechanochemical Control of Symmetry Breaking in the Caenorhabditis elegans Zygote."

Gan WJ, Motegi F

[Front Cell Dev Biol, 2020]

Cell polarity is the asymmetric organization of cellular components along defined axes. A key requirement for polarization is the ability of the cell to break symmetry and achieve a spatially biased organization. Despite different triggering cues in various systems, symmetry breaking (SB) usually relies on mechanochemical modulation of the actin cytoskeleton, which allows for advected movement and reorganization of cellular components. Here, the mechanisms underlying SB in <i>Caenorhabditis elegans</i> zygote, one of the most popular models to study cell polarity, are reviewed. A zygote initiates SB through the centrosome, which modulates mechanics of the cell cortex to establish advective flow of cortical proteins including the actin cytoskeleton and partitioning defective (PAR) proteins. The chemical signaling underlying centrosomal control of the Aurora A kinase-mediated cascade to convert the organization of the contractile actomyosin network from an apolar to polar state is also discussed.

Clarke ND et al. (1998) Science "Zinc fingers in Caenorhabditis elegans: finding families and probing pathways."

Berg JM, Clarke ND

[Science, 1998]

More than 3 percent of the protein sequences inferred from the Caenorhabditis elegans genome contain sequence motifs characteristic of zinc-binding structural domains, and of these more than half are believed to be sequence-specific DNA-binding proteins. The distribution of these zinc-binding domains among the genomes of various organisms offers insights into the role of zinc-binding proteins in evolution. In addition, the complete genome sequence of C. elegans provides an opportunity to analyze, and perhaps predict, pathways of transcriptional regulation.AD - Department of Biophysics and Biophysical Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.FAU - Clarke, N DAU - Clarke NDFAU - Berg, J MAU - Berg JMLA - engPT - Journal ArticlePT - ReviewPT - Review, TutorialCY - UNITED STATESTA - ScienceJID - 0404511RN - 0 (DNA-Binding Proteins)RN - 0 (Helminth Proteins)RN - 0 (Membrane Proteins)RN - 0 (Receptors, Cell Surface)RN - 0 (Trans-Activators)RN - 0 (Transcription Factors)RN - 0 (erythroid-like transcription factor 1)RN - 0 (tra-1 protein, Caenorhabditis elegans)SB - IM

Ruvkun GB et al. (1998) Science "The taxonomy of developmental control in Caenorhabditis elegans."

Ruvkun GB, Hobert O

[Science, 1998]

The Caenorhabditis elegans genome sequence was surveyed for transcription factor and signaling gene families that have been shown to regulate development in a variety of species. About 10 to 25 percent of the genes in most of the gene families already have been genetically analyzed in C. elegans, about half of the genes detect probable orthologs in other species, and about 10 to 25 percent of the genes are, at present, unique to C. elegans. Caenorhabditis elegans is also missing genes that are found in vertebrates and other invertebrates. Thus the genome sequence reveals universals in developmental control that are the legacy of metazoan complexity before the Cambrian explosion, as well as genes that have been more recently invented or lost in particular phylogenetic lineages.AD - Department of Molecular Biology, Massachusetts General Hospital, Department of Genetics, Harvard Medical School, Boston, MA 02114, USA. ruvkun@frodo.mgh.harvard.eduFAU - Ruvkun, GAU - Ruvkun GFAU - Hobert, OAU - Hobert OLA - engPT - Journal ArticlePT - ReviewPT - Review, TutorialCY - UNITED STATESTA - ScienceJID - 0404511RN - 0 (Helminth Proteins)RN - 0 (Transcription Factors)SB - IM