Chlorophyll synthesis in a deetiolated-(det340) mutant of Arabidopsis without NADPH-protochlorophyllide (PChlide) oxidoreductase (POR) A and photoactive PChlide-F655
Chlorophyll synthesis in a deetiolated-(det340) mutant of Arabidopsis without NADPH-protochlorophyllide (PChlide) oxidoreductase (POR) A and photoactive PChlide-F655
复制标题
DOI:
10.1105/tpc.7.12.2081
复制
发表时间:
1995-12-01
期刊:
影响因子:
11.6
通讯作者:
Apel, K
中科院分区:
文献类型:
--
作者:
Lebedev, N;vanCleve, B;Apel, K
Chlorophyll (Chl) synthesis in Arabidopsis is controlled by two light-dependent NADPH-protochlorophyllide (PChlide) oxidoreductases (PORs), one (FOR A) that is active transiently in etiolated seedlings at the beginning of illumination and another (FOR B) that also operates in green plants, The function of these two enzymes during the light-induced greening of dark-grown seedlings has been studied in the wild type and a deetiolated (det340) mutant of Arabidopsis. One of the consequences of the def mutation is that FOR A is constitutively down-regulated, and therefore, synthesis of the FOR A enzyme is shut off. When grown in the dark, the det340 mutant lacks FOR A and the photoactive PChlide-F655 species but maintains the second PChlide reductase, FOR B, Previously, photoactive PChlide-F655 has often been considered to be the only PChlide form that leads to Chi formation. Despite its deficiency in FOR A and photoactive PChlide-F655, the det340 mutant is able to green when placed in the light. Chi accumulation, however, proceeds abnormally, At the beginning of illumination, seedlings of det340 mutants are extremely susceptible to photooxidative damage and accumulate Chi only at extremely low light intensities, They form core complexes of photosystems I and II but are almost completely devoid of light-harvesting structures. The results of this study demonstrate that in addition to the route of Chi synthesis that has been studied extensively in illuminated dark-grown wild-type plants, a second branch of Chi synthesis exists that is driven by POR B and does not require POR A.