Molecular characterization of aldolase from Heterodera glycines and Globodera rostochiensis

• Published in: Journal of nematology Vol. 37; no. 3; pp. 292 - 296
• Main Authors: Kovaleva, E.S, Masler, E.P, Subbotin, S.A, Chitwood, D.J
• Format: Journal Article
• Language: English
• Published: United States Society of Nematologists 01.09.2005
• Subjects: aldolase gene; amino acid sequences; Biochemistry; complementary DNA; cyst nematodes; developmental stages; enzyme activity; enzyme inhibition; enzyme inhibitors; fructose-bisphosphate aldolase; Globodera rostochiensis; Heterodera glycines; introns; molecular sequence data; nucleotide sequences; sequence homology; enzyme; Heterodera; intron; Globodera; gene; cyst nematode; aldolase
• ISSN: 0022-300X; 2640-396X

Fructose-bisphosphate aldolase (EC 4.1.2.13) is a key enzyme in glycolysis. We have characterized full-length coding sequences for aldolase genes from the cyst nematodes Heterodera glycines and Globodera rostochiensis, the first for any plant-parasitic nematode. Nucleotide homology is high (83% identity), and the respective sequences encode 40 kDa proteins with 89% amino acid identity. Genomic sequences contain six introns located at identical positions in both genes. Intron 4 in the H. glycines gene is >500 bp. Partial genomic sequences determined for seven other cyst nematode species reveal that the large fourth intron is characteristic of Heterodera but not Globodera aldolase genes. Total aldolase-like specific activity in homogenates from H. glycines was 2-fold lower than in either Caenorhabditis elegans or Panagrellus redivivus (P = 0.001). Activity in H. glycines samples was higher in juvenile stages than in adults (P = 0.003). Heterodera glycines aldolase has Km = 41 micromolar and is inhibited by treatment with carboxypeptidase A or sodium borohydride.