Inhibition of the light-independent synthesis of chlorophyll in pine cotyledons at low temperature.
Cotyledons of Japanese black pine (Pinus thunbergii) were yellow when they developed in darkness at 8 degrees C since the light-independent synthesis of chlorophyll was almost completely inhibited in these cotyledons. The level of chlorophyll in dark-grown cotyledons was less than one-twentieth of that in light-grown cotyledons at the same temperature. In the yellow cotyledons, levels of transcripts of cab, rbcS, rbcL and psbA genes were quite high. The large and small subunits of ribulose-1,5-bisphosphate carboxylase/oxygenase were also detected at relatively high levels in yellow cotyledons. However, the accumulation of the two apoproteins of the light-harvesting chlorophyll a/b-binding protein of PSII was limited because of the limited supply of chlorophyll.
Muramatsu
S
S
Department of Molecular and Cell Biology, Forestry and Forest Products Research Institute, Ibaraki, 305-8687 Japan.
Kojima
K
K
Igasaki
T
T
Azumi
Y
Y
Shinohara
K
K
D002734:Chlorophyll / Q000096:biosynthesis*; D003080:Cold Temperature; D018548:Cotyledon / Q000254:growth & development / Q000378:metabolism*; D032462:Cycadopsida / Q000254:growth & development / Q000378:metabolism* / Q000528:radiation effects; D003624:Darkness; D018506:Gene Expression Regulation, Plant; D018525:Germination; D008027:Light; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism; D015533:Transcriptional Activation
D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D002734:Chlorophyll; D012273:Ribulose-Bisphosphate Carboxylase