Abstract
As compared with normal wheat leaves, the chlorina wheat mutant, designated CD3, has a high chlorophyll a/b ratio and a deficiency in the light harvesting chlorophyll protein (LHCP) complex. Applications of 200 micrograms per milliliter of d-threo-chloramphenicol to etiolated seedlings decreased the chlorophyll a/b ratio and increased the accumulation of the 27 kilodalton LHCP polypeptide and the LHCP complex in thylakoids of the mutant during greening. These data led to the suggestion that a protein encoded in chloroplast genes impaired either transcriptional, translational, or posttranslational events in CD3 wheat limiting the accumulation of the LHCP complex. The LHCP complex which accumulated in chloramphenicol treated wheat appeared functional even though chlorophyll protein complex accumulations were altered greatly in the wheat thylakoids. LHCP polypeptides were phosphorylated by action of a membrane protein kinase but yet photosystem II electron transport was impaired. The chloramphenicol treatment increased the photosystem I/photosystem II ratio of electron transport and the fluorescence emission ratio at 740 to 686 nanometers relative to those of untreated wheat. Chloramphenicol prevented development of normal granal thylakoids in normal wheat chloroplasts but not in those of the CD3 mutant. Elongated stacked thylakoids were observed in normal wheat. Net-like membranes and vesicles were noted in the stroma of chloroplasts from treated mutant seedlings.
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