Aspartic proteases from the nematode Caenorhabditis elegans: Structural organization and developmental and cell-specific expression of asp-1

Irina Tcherepanova, Lokesh Bhattacharyya, Charles S. Rubin, Jonathan H. Freedman

Research output: Contribution to journalArticle

51 Scopus citations

Abstract

A Caenorhabditis elegans gene (asp-1) and cDNA that encode a homologue of cathepsin D aspartic protease were cloned and characterized. The asp-1 mRNA is transcribed from a single exon, and it begins with the SL1 trans-splice leader sequence. The protein (ASP-1) is expressed as a 396-amino acid, 42.7-kDa pre-pro-peptide that is post-translationally processed into a ~40-kDa lysosomal protein. ASP-1 shares ~60% sequence identity with the aspartic protease precursor from the nematode Strongyloides stercoralis. The amino acid sequences adjacent to the two active site aspartic acid residues in ASP-1 are 100% identical to those in other eukaryotic aspartic proteases. In addition, ASP-1 contains conserved, potential disulfide bond-forming cysteine residues and N-glycosylation sites. The asp-1 gene is exclusively transcribed in the intestinal cells, with the highest levels of expression observed at late embryonic and early larval stages of development, asp-1 transcription is not observed in adult nematodes or mature larvae. Furthermore, transcription predominantly occurs in eight anterior cells of the intestine (int6-int8). Analyses of ASP-1 nucleotide and amino acid sequences revealed the presence of five additional C. elegans aspartic proteases.

Original languageEnglish (US)
Pages (from-to)26359-26369
Number of pages11
JournalJournal of Biological Chemistry
Volume275
Issue number34
DOIs
StatePublished - Aug 25 2000

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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