TABLE 1

High-temperature anoxia phenotype of the daf-2(e1370);glycolytic gene(RNAi)

Metabolic enzyme (sequence name, gene)% survival anoxia at 28° (% ±SD)Predicted enzymatic activity
HexokinaseGlucose + ATP → glucose-6-phosphate + ADP
    F14B4.2100.0 ± 0
    H25P06.199.0 ± 1.4
    Y77E11A.184.0 ± 12.4
Glucose phosphate isomeraseGlucose-6-phosphate → fructose-6-phosphate
    Y87G2A.8, gpi-1100.0 ± 0
PhosphofructokinaseFructose-6-phosphate → fructose-1,6-bisphosphate
    Y71H10A.189.9 ± 11.3
    C50F4.298.0 ± 2.0
Fructose-1,6-bisphosphate aldolaseFructose-1,6-bisphosphate → glyceraldehyde-3-phosphate, dihydroxyacetone phosphate
    F01F1.1299.1 ± 1.5
    T05D4.193.6 ± 5.5
Triose phosphate isomeraseDihydroxyacetone phosphate → glyceraldehyde-3-phosphate
    Y17G7B.7, tpi-199.0 ± 1.2
Glyceraldehyde-3-phosphate dehydrogenaseGlyceraldehyde-3-phosphate + NAD + Pi → 1,3-bisphosphoglycerate + NADH
    T09F3.3, gpd-195.3 ± 5.1
    K10B3.8, gpd-236.7 ± 16.8*
    K10B3.7, gpd-36.0 ± 6.0*
    F33H1.2, gpd-498.6 ± 1.5
Phosphoglycerate kinase1,3-Bisphosphoglycerate + ADP → 3-phosphoglycerate + ATP
    T03F1.3, pgk-1100 ± 0
Phosphoglycerate mutase3-Phosphoglycerate → 2-phosphoglycerate
    F53B6.798.7 ± 2.3
    R07G3.595.5 ± 5.3
    F55A11.1196.8 ± 5.6
    T07F12.1100 ± 0
    F09C12.8100 ± 0
Enolase2-Phosphoglycerate → phosphoenolpyruvate + H2O
    T21B10.2, enol-194.3 ± 6.4
Pyruvate kinasePhosphoenolpyruvate + ADP → pyruvate + ATP
    F25H5.399.3 ± 1.5
    ZK593.198 ± 1.6
Control vector98.4 ± .9
  • The daf-2(e1370) animal was fed a specific bacterial clone to inhibit the gene expression of interest. For all data sets, three independent experiments of at least 50 worms were tested. * P < 0.001, as determined by ANOVA or Student's t-test.