Literature DB >> 1574082

Gut-specific and developmental expression of a Caenorhabditis elegans cysteine protease gene.

C Ray1, J H McKerrow.   

Abstract

A Caenorhabditis elegans cysteine protease gene fragment, amplified by PCR using conserved eukaryotic protease gene sequences as primers, was used as a probe to isolate cDNA and genomic clones. The genomic clone, which had a coding sequence of 987 bp interrupted by 2 small introns, was physically mapped to the middle of linkage group V. The predicted amino acid sequence of the mature C. elegans cysteine protease was homologous to those of other eukaryotic cysteine proteases, particularly to that of the nematode parasite Haemonchus contortus (50%) and to the cathepsin B-like hemoglobinase of the trematode parasite Schistosoma mansoni (54%). The pro region of the C. elegans protease was homologous only to that of the H. contortus enzyme, implying a similar mechanism of protease activation. The C. elegans cysteine protease gene was temporally regulated: abundant 1.1-kb transcripts were detected in larvae and adults, but not in embryos. Transcription also was spatially regulated, occurring only in the intestine. Like the vitellogenin genes, which also are transcribed exclusively in the intestine, the 5' end of the C. elegans cysteine protease gene had at least one copy of each of 2 heptameric sequences which may be transcriptional regulatory elements governing gut-specific expression.

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Year:  1992        PMID: 1574082     DOI: 10.1016/0166-6851(92)90074-t

Source DB:  PubMed          Journal:  Mol Biochem Parasitol        ISSN: 0166-6851            Impact factor:   1.759


  11 in total

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3.  Chromosomal clustering and GATA transcriptional regulation of intestine-expressed genes in C. elegans.

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4.  New nucleotide sequence data on the EMBL File Server.

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Journal:  Nucleic Acids Res       Date:  1992-06-11       Impact factor: 16.971

5.  Molecular and biochemical characterization of hemoglobinase, a cysteine proteinase, in Paragonimus westermani.

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10.  Cathepsin B Cysteine Proteinase is Essential for the Development and Pathogenesis of the Plant Parasitic Nematode Radopholus similis.

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