Characterization of Mutations Induced by Ethyl Methanesulfonate, UV, and Trimethylpsoralen in the Nematode Caenorhabditis elegans

ABSTRACT Six schemes were used to identify 80 independent recessive lethal deficiencies of linkage group (LG) II following X-ray treatment of the nematode Caenorhabditis elegans. Complementation tests between the deficiencies and ethyl methanesulfonate-induced recessive visible, lethal and sterile mutations and between different deficiencies were used to characterize the extents of the deficiencies. Deficiency endpoints thus helped to order 36 sites within a region representing about half of the loci on LG II and extending over about 5 map units. New mutations occurring in this region can be assigned to particular segments of the map by complementation tests against a small number of deficiencies; this facilitates the assignment of single-site mutations to particular genes, as we illustrate. Five sperm-defective and five oocyte-defective LG II sterile mutants were identified and mapped. Certain deficiency-by-deficiency complementation tests allowed us to suggest that the phenotypes of null mutations at two loci represented by visible alleles are wild type and that null mutations at a third locus confer a visible phenotype. A segment of LG II that is about 12 map units long and largely devoid of identified loci seems to be greatly favored for crossing over.

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Cloning and biochemical characterization of the cyclophilin homologues from the free-living nematode Caenorhabditis elegans

Biochemical Journal ◽

10.1042/bj3170179 ◽

1996 ◽

Vol 317 (1) ◽

pp. 179-185 ◽

Cited By ~ 43

Author(s):

Antony P. PAGE ◽

Kenneth MacNIVEN ◽

Michael O. HENGARTNER

Keyword(s):

Signal Transduction ◽

Protein Folding ◽

Caenorhabditis Elegans ◽

Biochemical Characterization ◽

Single Species ◽

Immunosuppressive Agent ◽

Specific Substrate ◽

Nematode Caenorhabditis Elegans ◽

Isomerase Activity

Cyclosporin A (CsA) is the most widely used immunosuppressive agent, whose properties are exerted via an interaction with cyclophilin, resulting in down-regulation of signal-transduction events in the T-cell. Cyclophilin is identical with peptidylprolyl cis–trans isomerase (PPI; EC 5.2.1.8), an enzyme which catalyses the isomerization between the two proline conformations in proteins, thereby acting as a catalyst in protein-folding events. Several reports indicate that CsA has potent anti-parasitic activity, effective against both protozoan and helminth species. In order to understand the various biological roles that cyclophilins play we have initiated a study of these proteins in the genetically tractable nematode Caenorhabditis elegans. Here we describe the cloning and characterization of 11 cyclophilin genes (cyp-1 to -11) derived from this nematode; this is currently the greatest number of isoforms described in a single species. Southern blotting and physical mapping indicated that these genes are dispersed throughout the nematode genome. A high degree of conservation exists between several isoforms, which also share characteristics with the ubiquitous isoforms previously described. The remaining isoforms are divergent, having altered CsA-binding domains and additional non-cyclophilin domains, which may impart compartmental specificity. Ten of these isoforms have been expressed in Escherichia coli, and the resultant fusion proteins have been examined biochemically for PPI activity, which they all possess. Isomerase activity is highest in the conserved and lowest in divergent isoforms, perhaps indicating a more specific substrate for the latter. Analysis of the C. elegans cyp genes will provide answers as to the roles played by cyclophilins in protein folding and signal transduction.

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Isolatio and characterization of metallothionein from nematode(Caenorhabditis elegans)

Eisei kagaku ◽

10.1248/jhs1956.32.22 ◽

1986 ◽

Vol 32 (1) ◽

pp. 22-27 ◽

Cited By ~ 7

Author(s):

KOHJI MARUYAMA ◽

RITSUKO HORI ◽

TSUTOMU NISHIHARA ◽

MASAOMI KONDO

Keyword(s):

Caenorhabditis Elegans ◽

Nematode Caenorhabditis Elegans

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Viable maternal-effect mutations that affect the development of the nematode Caenorhabditis elegans.

Genetics ◽

10.1093/genetics/141.4.1351 ◽

1995 ◽

Vol 141 (4) ◽

pp. 1351-1364 ◽

Cited By ~ 8

Author(s):

S Hekimi ◽

P Boutis ◽

B Lakowski

Keyword(s):

Quantitative Analysis ◽

Caenorhabditis Elegans ◽

Maternal Effect ◽

Genetic Screen ◽

Phenotypic Characterization ◽

Nematode Caenorhabditis Elegans ◽

Critical Function ◽

Complementation Groups

Abstract We carried out a genetic screen for viable maternal-effect mutants to identify genes with a critical function relatively early in development. This type of mutation would not have been identified readily in previous screens for viable mutants and therefore could define previously unidentified genes. We screened 30,000 genomes and identified 41 mutations falling into 24 complementation groups. We genetically mapped these 24 loci; only two of them appear to correspond to previously identified genes. We present a partial phenotypic characterization of the mutants and a quantitative analysis of the degree to which they can be maternally or zygotically rescued.

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Genetic and Molecular Characterization of Ca2+ and IP3 Signaling in the Nematode Caenorhabditis elegans

Calcium Signaling, Second Edition ◽

10.1201/9781420038231.ch8 ◽

2005 ◽

pp. 161-186

Author(s):

Kevin Strange ◽

Ana Estevez

Keyword(s):

Caenorhabditis Elegans ◽

Molecular Characterization ◽

Nematode Caenorhabditis Elegans

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IDENTIFICATION AND CHARACTERIZATION OF 22 GENES THAT AFFECT THE VULVAL CELL LINEAGES OF THE NEMATODE CAENORHABDITIS ELEGANS

Genetics ◽

10.1093/genetics/110.1.17 ◽

1985 ◽

Vol 110 (1) ◽

pp. 17-72

Author(s):

Edwin L Ferguson ◽

H Robert Horvitz

Keyword(s):

Caenorhabditis Elegans ◽

Gene Function ◽

Ventral Side ◽

Recessive Mutation ◽

Partial Reduction ◽

Nematode Caenorhabditis Elegans ◽

Multiple Alleles ◽

Cell Lineages ◽

Identification And Characterization

ABSTRACT Ninety-five mutants of the nematode Caenorhabditis elegans altered in the cell lineages of the vulva have been isolated on the basis of their displaying one of two phenotypes, Vulvaless or Multivulva. In Vulvaless mutants, which define 12 genes, no vulva is present. In Multivulva mutants, which define ten genes, one or more supernumerary vulva-like protrusions are located along the ventral side of the animal. A single recessive mutation is responsible for the phenotypes of most, but not all, of these strains. Fifteen of these 22 genes are represented by multiple alleles. We have shown by a variety of genetic criteria that mutations that result in a Vulvaless or Multivulva phenotype in six of the 22 genes most likely eliminate gene function. In addition, Vulvaless or Multivulva mutations in seven of the other genes most likely result in a partial reduction of gene function; the absence of the activity of any of these genes probably results in lethality or sterility. Our results suggest that we may have identified most, or all, genes of these two classes.

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Characterization of N-Acyl Phosphatidylethanolamine-Specific Phospholipase-D Isoforms in the Nematode Caenorhabditis elegans

PLoS ONE ◽

10.1371/journal.pone.0113007 ◽

2014 ◽

Vol 9 (11) ◽

pp. e113007 ◽

Cited By ~ 7

Author(s):

Neale Harrison ◽

Museer A. Lone ◽

Tiffany K. Kaul ◽

Pedro Reis Rodrigues ◽

Ifedayo Victor Ogungbe ◽

...

Keyword(s):

Caenorhabditis Elegans ◽

Phospholipase D ◽

Nematode Caenorhabditis Elegans

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Molecular basis of loss-of-function mutations in the glp-1 gene of Caenorhabditis elegans.

Molecular Biology of the Cell ◽

10.1091/mbc.3.11.1199 ◽

1992 ◽

Vol 3 (11) ◽

pp. 1199-1213 ◽

Cited By ~ 75

Author(s):

V Kodoyianni ◽

E M Maine ◽

J Kimble

Keyword(s):

Caenorhabditis Elegans ◽

Growth Factor ◽

Molecular Basis ◽

Missense Mutations ◽

Loss Of Function ◽

Nematode Caenorhabditis Elegans ◽

Nonsense Mutations ◽

Epidermal Growth ◽

Repeated Motifs

The glp-1 gene encodes a membrane protein required for inductive cell interactions during development of the nematode Caenorhabditis elegans. Here we report the molecular characterization of 15 loss-of-function (lf) mutations of glp-1. Two nonsense mutations appear to eliminate glp-1 activity; both truncate the glp-1 protein in its extracellular domain and have a strong loss-of-function phenotype. Twelve missense mutations and one in-frame deletion map to sites within the repeated motifs of the glp-1 protein (10 epidermal growth factor [EGF]-like and 3 LNG repeats extracellularly and 6 cdc10/SWI6, or ankyrin, repeats intracellularly). We find that all three types of repeated motifs are critical to glp-1 function, and two individual EGF-like repeats may have distinct functions. Intriguingly, all four missense mutations in one phenotypic class map to the N-terminal EGF-like repeats and all six missense mutations in a second phenotypic class reside in the intracellular cdc10/SWI6 repeats. These two clusters of mutations may identify functional domains within the glp-1 protein.

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