Assessing the function of the Ro ribonucleoprotein complex using<i> Caenorhabditis elegans</i> as a biological tool

Jean-Claude Labbé; Siegfried Hekimi; Luis A. Rokeach

doi:10.1139/bcb-77-4-349

Assessing the function of the Ro ribonucleoprotein complex using Caenorhabditis elegans as a biological tool

Biochemistry and Cell Biology ◽

10.1139/bcb-77-4-349 ◽

1999 ◽

Vol 77 (4) ◽

pp. 349-354 ◽

Cited By ~ 2

Author(s):

Jean-Claude Labbé ◽

Siegfried Hekimi ◽

Luis A. Rokeach

Keyword(s):

Caenorhabditis Elegans ◽

Ribonucleoprotein Complex ◽

Biological Tool ◽

Ro Ribonucleoprotein

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Assessing the function of the Ro ribonucleoprotein complex using Caenorhabditis elegans as a biological tool

Biochemistry and Cell Biology ◽

10.1139/o99-036 ◽

1999 ◽

Vol 77 (4) ◽

pp. 349-354 ◽

Cited By ~ 3

Author(s):

Jean-Claude Labbé ◽

Siegfried Hekimi ◽

Luis A Rokeach

Keyword(s):

Caenorhabditis Elegans ◽

Lupus Erythematosus ◽

Ribosome Biogenesis ◽

General Structure ◽

Major Protein ◽

Phenotypic Analysis ◽

Gene Encoding ◽

Ribonucleoprotein Complex ◽

Biological Tool ◽

Ro Ribonucleoprotein

The Ro ribonucleoprotein complex (Ro RNP) was initially described as an autoimmune target in human diseases such as systemic lupus erythematosus and Sjögren's syndrome. In Xenopus and human cells, its general structure is composed of one major protein of 60 kDa, Ro60, that binds to one of four small RNA molecules, designated Y RNAs. Although no function has been assigned to the Ro RNP, Ro60 has been shown to bind mutant 5S ribosomal RNA (rRNA) molecules in Xenopus oocytes, suggesting a role for Ro60 in 5S rRNA biogenesis. Ro60 has also been shown to participate in the regulation of the translational fate of the L4 ribosomal protein mRNA by interacting with the 5prime untranslated region, again suggesting its possible implication in ribosome biogenesis. To identify the function of Ro RNP, we have taken a genetic approach in the nematode Caenorhabditis elegans. As such, we characterized the gene encoding the protein ROP-1, the homologue of the human Ro60 protein. Here, we review the phenotypic analysis of C. elegans rop-1(-) mutants and integrate these results into a model for the function of the Ro RNP particle.Key words: Caenorhabditis elegans, Ro ribonucleoprotein complex, ROP-1, small RNAs, quality control.

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Review for "The connectome of the Caenorhabditis elegans pharynx"

10.1002/cne.24932/v1/review1 ◽

2020 ◽

Author(s):

Sreekanth Chalasani

Keyword(s):

Caenorhabditis Elegans

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The glycomes of Caenorhabditis elegans and other model organisms

Biochemical Society Symposium ◽

10.1042/bss0690117 ◽

2002 ◽

Vol 69 ◽

pp. 117-134 ◽

Cited By ~ 47

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.

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