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Human proprotein convertase 2 homologue from a plant nematode: Cloning, characterization, and comparison with other species
Author(s) -
Kovaleva Elena S.,
Yakovlev Alexander G.,
Masler Edward P.,
Chitwood David J.
Publication year - 2002
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.01-0940fje
Subject(s) - proprotein convertases , biology , signal peptide , catalytic triad , nematode , complementary dna , biochemistry , caenorhabditis elegans , peptide sequence , amino acid , in silico , pentapeptide repeat , gene , peptide , genetics , lipoprotein , ecology , ldl receptor , cholesterol
Proprotein convertases (PCs) are evolutionarily conserved enzymes responsible for processing the precursors of many bioactive peptides in mammals. The invertebrate homologues of PC2 play important roles during development that makes the enzyme a good target for practical applications in pest management. Screening of a plant nematode Heterodera glycines cDNA library resulted in isolation of a full‐length clone encoding a PC2‐like precursor. The deduced protein (74.2 kD) exhibits strong amino acid homology to all known PC2s, including human, and shares the main structural characteristics: signal peptide; prosegment; catalytic domain, with D/H/S catalytic triad, PC2‐specific residues, and 7B2 binding sites; P domain (with RRGDT pentapeptide); and carboxyl terminus. Comparative analysis of PC2s from 15 species discloses the presence of an insert in the catalytic domain unique to nematodes. Expression of PC2‐like mRNA found in eggs and juveniles was undetectable in adult stages of H. glycines . Nucleotide analysis reveals distinctive differences in base composition and codon usage between H. glycines and Caenorhabditis elegans PC2s. The H. glycines cDNA clone encoding PC2 is the first one isolated from plant‐parasitic nematodes.