Amoebapore homologs of Caenorhabditis elegans

It is shown that the Caenorhabditis elegans genome contains several distantly related members of the gene family of saposin-like proteins. The putative products of genes T07C4.4, T08A9.7A, T08A9.7B, T08A9.8, T08A9.9, T08A9.10 are similar to the amoebapores of Entamoeba histolytica, granulysin of cyt...

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Bibliographic Details
Published in:Biochimica et biophysica acta 1998-12, Vol.1429 (1), p.259-264
Main Authors: Bányai, László, Patthy, László
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amoebapore
Animals
Base Sequence
Caenorhabditis elegans
Caenorhabditis elegans - genetics
Caenorhabditis elegans Proteins
Circular Dichroism
Entamoeba histolytica - genetics
Glycoproteins - genetics
Granulysin
Helminth Proteins - chemistry
Helminth Proteins - genetics
Molecular Sequence Data
NK-lysin
Protein Sorting Signals - genetics
Saposin-like domain
Saposins
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Summary:It is shown that the Caenorhabditis elegans genome contains several distantly related members of the gene family of saposin-like proteins. The putative products of genes T07C4.4, T08A9.7A, T08A9.7B, T08A9.8, T08A9.9, T08A9.10 are similar to the amoebapores of Entamoeba histolytica, granulysin of cytotoxic T lymphocytes and a putative amoebapore-related protein of the liver fluke Fasciola hepatica inasmuch as they consist of only a single saposin-like domain and a secretory signal peptide. The saposin-like domain of protein T07C4.4, which is most closely related to NK-lysin and granulysin, has been expressed in Escherichia coli and the recombinant protein was shown to have a circular dichroism spectrum consistent with the helix bundle structure characteristic of saposin-like domains. Recombinant T07C4.4 protein was found to have antibacterial activity, suggesting that these amoebapore homologs may play a role in antibacterial mechanisms of C. elegans.
ISSN:0167-4838
0006-3002
1879-2588
DOI:10.1016/S0167-4838(98)00237-4