Genetic and biochemical analysis of anaerobically-induced enzymes during seed germination of Echinochloa crus-galli varieties tolerant and intolerant of anoxia.
To compare the regulation of anaerobic metabolism during germination in anoxia-tolerant and intolerant plants, enzymes associated with anaerobic metabolism such as sucrose synthase, aldolase, enolase, pyruvate decarboxylase (PDC), alcohol dehydrogenase (ADH), and aldehyde dehydrogenase (ALDH) were assayed in two varieties of Echinochloa crus-galli, formosensis (tolerant) and praticola (intolerant). The initial and intervening enzymes of the pathway (sucrose synthase and aldolase) and enzymes in the last part of the pathway (PDC, ADH and ALDH) revealed similar changing patterns in activities during germination. This implies that each group of enzymes may be controlled by an identical regulatory mechanism. During anoxia, activities of all enzymes increased 1.5-30-fold in both varieties compared to their activities under aerobic conditions. Activities of sucrose synthase, enolase and ADH exhibited the same induction patterns under anoxia in formosensis and praticola. However, the activities of aldolase, ALDH and PDC were more strongly induced in formosensis under anoxia (1.2-2-fold) than in praticola. These enzymes were also assayed in F(3) families which varied in their anaerobic germinability. For PDC, activities under anoxia in anoxia-tolerant families were similar to those of an anoxia-intolerant family during the whole period although the family did not exhibit anaerobic germinability. This suggests that there is no correlation between PDC activity and anaerobic germinability. For ALDH, activities were more strongly induced under anoxia in anoxia-tolerant families than in anoxia-intolerant families, a trend also exhibited by the parents. This indicates that ALDH may play a role in detoxifying acetaldehyde formed through alcoholic fermentation during anaerobic germination.
Fukao
Takeshi
T
Department of Horticultural Sciences, Texas A&M University, College Station, TX 77843, USA.
Kennedy
Robert A
RA
Yamasue
Yuji
Y
Rumpho
Mary E
ME
D000222:Adaptation, Physiological / Q000187:drug effects / Q000502:physiology; D000332:Aerobiosis; D000426:Alcohol Dehydrogenase / Q000096:biosynthesis; D000444:Aldehyde Dehydrogenase / Q000096:biosynthesis; D000693:Anaerobiosis; D031747:Echinochloa / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D004790:Enzyme Induction / Q000187:drug effects; D004798:Enzymes / Q000096:biosynthesis*; D005634:Fructose-Bisphosphate Aldolase / Q000096:biosynthesis; D005816:Genetic Complementation Test; D018525:Germination / Q000187:drug effects / Q000235:genetics / Q000502:physiology; D005964:Glucosyltransferases / Q000096:biosynthesis; D007527:Isoenzymes / Q000096:biosynthesis; D010100:Oxygen / Q000494:pharmacology*; D010751:Phosphopyruvate Hydratase / Q000096:biosynthesis; D011767:Pyruvate Decarboxylase / Q000096:biosynthesis; D012639:Seeds / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D014867:Water / Q000494:pharmacology
D004798:Enzymes; D007527:Isoenzymes; D014867:Water; D000426:Alcohol Dehydrogenase; D000444:Aldehyde Dehydrogenase; D005964:Glucosyltransferases; C022699:sucrose synthase; D011767:Pyruvate Decarboxylase; D005634:Fructose-Bisphosphate Aldolase; D010751:Phosphopyruvate Hydratase; D010100:Oxygen