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 |
|---|---|---|
| Hexokinase | Glucose + ATP → glucose-6-phosphate + ADP | |
| F14B4.2 | 100.0 ± 0 | |
| H25P06.1 | 99.0 ± 1.4 | |
| Y77E11A.1 | 84.0 ± 12.4 | |
| Glucose phosphate isomerase | Glucose-6-phosphate → fructose-6-phosphate | |
| Y87G2A.8, gpi-1 | 100.0 ± 0 | |
| Phosphofructokinase | Fructose-6-phosphate → fructose-1,6-bisphosphate | |
| Y71H10A.1 | 89.9 ± 11.3 | |
| C50F4.2 | 98.0 ± 2.0 | |
| Fructose-1,6-bisphosphate aldolase | Fructose-1,6-bisphosphate → glyceraldehyde-3-phosphate, dihydroxyacetone phosphate | |
| F01F1.12 | 99.1 ± 1.5 | |
| T05D4.1 | 93.6 ± 5.5 | |
| Triose phosphate isomerase | Dihydroxyacetone phosphate → glyceraldehyde-3-phosphate | |
| Y17G7B.7, tpi-1 | 99.0 ± 1.2 | |
| Glyceraldehyde-3-phosphate dehydrogenase | Glyceraldehyde-3-phosphate + NAD + Pi → 1,3-bisphosphoglycerate + NADH | |
| T09F3.3, gpd-1 | 95.3 ± 5.1 | |
| K10B3.8, gpd-2 | 36.7 ± 16.8* | |
| K10B3.7, gpd-3 | 6.0 ± 6.0* | |
| F33H1.2, gpd-4 | 98.6 ± 1.5 | |
| Phosphoglycerate kinase | 1,3-Bisphosphoglycerate + ADP → 3-phosphoglycerate + ATP | |
| T03F1.3, pgk-1 | 100 ± 0 | |
| Phosphoglycerate mutase | 3-Phosphoglycerate → 2-phosphoglycerate | |
| F53B6.7 | 98.7 ± 2.3 | |
| R07G3.5 | 95.5 ± 5.3 | |
| F55A11.11 | 96.8 ± 5.6 | |
| T07F12.1 | 100 ± 0 | |
| F09C12.8 | 100 ± 0 | |
| Enolase | 2-Phosphoglycerate → phosphoenolpyruvate + H2O | |
| T21B10.2, enol-1 | 94.3 ± 6.4 | |
| Pyruvate kinase | Phosphoenolpyruvate + ADP → pyruvate + ATP | |
| F25H5.3 | 99.3 ± 1.5 | |
| ZK593.1 | 98 ± 1.6 | |
| Control vector | 98.4 ± .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.