Molecular and genetic analyses of the Caenorhabditis elegans dpy-2 and dpy-10 collagen genes: a variety of molecular alterations affect organismal morphology.

Levy, Adam D.; Yang, Jie; Kramer, James M.

doi:10.1091/mbc.4.8.803

Cited by 91 publications

(74 citation statements)

References 59 publications

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“…In addition, 33 mutations in seven different cuticle collagen genes of C. elegans have been reported (Johnstone et al, 1992;Kramer, 1993;Kramer and Johnson, 1993;Levy et al, 1993; this paper), as well as 20 mutations in the two basement membrane collagen genes (Guo et al, 1991;Kramer, 1993). In the cuticle mutants, most of which were isolated after EMS treatment, glycine is replaced by either aspartic acid, glutamic acid, or arginine.…”

Section: Discussionmentioning

confidence: 82%

Caenorhabditis elegans sqt‐3 mutants have mutations in the col‐1 collagen gene

Keyl

Kim

Espey

et al. 1994

Developmental Dynamics

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ABSTRACTsqt-3 mutants of Caenorhabditis elegans form dumpy larvae and adults and display allele-specific defects in locomotion, fertility, and viability. We have determined that the sqt-3 locus encodes COL-1 collagen. We physically mapped the col-1 gene to a cosmid on chromosome V whose position is consistent with the location of the sqt-3 gene. We also observed morphological defects in sqt-3 mutants at stages that correlate with the mRNA expression patterns of col-1. Sequence analysis of the col-1 gene in the three temperature-sensitive mutants revealed that each allele of sqt-3 has a unique missense mutation causing arginine or glutamic acid to replace glycine in a Gly-X-Y triple helical domain. These glycine substitutions may result in longer non-collagenous domains, which may decrease the thermal stability or impart additional flexibility to mutant trimers. In addition, we describe four corrections to the published sequence of col-1, including one fifteen nucleotide addition that completes a conserved domain in the amino terminal coding region. 0 1994 Wiley-Liss, Inc.

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Section: Discussionmentioning

confidence: 82%

Caenorhabditis elegans sqt‐3 mutants have mutations in the col‐1 collagen gene

Keyl

Kim

Espey

et al. 1994

Developmental Dynamics

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“…Likewise, limited secretion of SQT-3 was detected in dpy-17(e164) animals raised at 15°(data not shown). To confirm that intracellular retention of SQT-3 is specific to dpy-17(0) mutants, we tested SQT-3 immunolocalization in dpy-7(e88), dpy-10(e128), and dpy-13(e184) cuticle collagen mutants (von Mende et al 1988;Johnstone et al 1992;Levy et al 1993). In all cases, SQT-3 is secreted and assembles in the cuticle normally at 20° (Figure 9).…”

Section: Resultsmentioning

confidence: 95%

The C Terminus of Collagen SQT-3 Has Complex and Essential Functions in Nematode Collagen Assembly

Novelli

Page²,

Hodgkin

2006

Genetics

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The nematode exoskeleton is a multilayered structure secreted by the underlying hypodermal cells and mainly composed of small collagens, which are encoded by a large gene family. In previous work, we reported analysis of the C. elegans dpy-31 locus, encoding a hypodermally expressed zinc-metalloprotease of the BMP-1/TOLLOID family essential for viability and cuticle deposition. We have generated a large set of extragenic suppressors of dpy-31 lethality, most of which we show here to be allelic to the cuticle collagen genes sqt-3 and dpy-17. We analyzed the interaction among dpy-31, sqt-3, and dpy-17 using a SQT-3-specific antiserum, which was employed in immunofluorescence experiments. Our results support a role for DPY-31 in SQT-3 extracellular processing and suggest that the SQT-3 C-terminal nontrimeric region serves multiple roles during SQT-3 assembly. Different missense mutations of this region have diverse phenotypic consequences, including cold-sensitive lethality. Furthermore, the biochemical and genetic data indicate that the extracellular assemblies of DPY-17 and SQT-3 are interdependent, most likely because the collagens are incorporated into the same cuticular substructure. We find that absence of DPY-17 causes extensive intracellular retention of SQT-3, indicating that formation of the SQT-3-DPY-17 polymer could begin in the intracellular environment before secretion.

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“…A spontaneous mutation in dpy-10 was isolated from the clk-2(mn159) mutant background, and analysis of the dpy-10 locus (Levy et al 1993) revealed a 3.616-kb deletion and a long 42-bp G/Crich sequence located near one deletion breakpoint (Table 1, Figure 1). Thus, five of six spontaneous mrt-2-induced mutations and one spontaneous clk-2-induced mutation resulted from deletions, three of which displayed G-or G/C-rich sequences near one deletion breakpoint.…”

Section: Resultsmentioning

confidence: 99%

Mutator Phenotype ofCaenorhabditis elegansDNA Damage Checkpoint Mutants

Harris¹,

Lowden²,

Clejan

et al. 2006

Genetics

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DNA damage response proteins identify sites of DNA damage and signal to downstream effectors that orchestrate either apoptosis or arrest of the cell cycle and DNA repair. The C. elegans DNA damage response mutants mrt-2, hus-1, and clk-2(mn159) displayed 8-to 15-fold increases in the frequency of spontaneous mutation in their germlines. Many of these mutations were small-to medium-sized deletions, some of which had unusual sequences at their breakpoints such as purine-rich tracts or direct or inverted repeats. Although DNA-damage-induced apoptosis is abrogated in the mrt-2, hus-1, and clk-2 mutant backgrounds, lack of the apoptotic branch of the DNA damage response pathway in cep-1/p53, ced-3, and ced-4 mutants did not result in a Mutator phenotype. Thus, DNA damage checkpoint proteins suppress the frequency of mutation by ensuring that spontaneous DNA damage is accurately repaired in C. elegans germ cells. Although DNA damage response defects that predispose humans to cancer are known to result in large-scale chromosome aberrations, our results suggest that small-to medium-sized deletions may also play roles in the development of cancer.

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Molecular and genetic analyses of the Caenorhabditis elegans dpy-2 and dpy-10 collagen genes: a variety of molecular alterations affect organismal morphology.

Cited by 91 publications

References 59 publications

Caenorhabditis elegans sqt‐3 mutants have mutations in the col‐1 collagen gene

Caenorhabditis elegans sqt‐3 mutants have mutations in the col‐1 collagen gene

The C Terminus of Collagen SQT-3 Has Complex and Essential Functions in Nematode Collagen Assembly

Mutator Phenotype ofCaenorhabditis elegansDNA Damage Checkpoint Mutants

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