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Synthesis and turnover of the light-harvesting chlorophyll a/b-protein in Lemna gibba grown with intermittent red light: possible translational control
Synthesis and turnover of the light-harvesting chlorophyll a/b-protein in Lemna gibba grown with intermittent red light: possible translational control
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Synthesis and turnover of the light-harvesting chlorophyll a/b-protein in Lemna gibba grown with intermittent red light: possible translational control
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Synthesis and turnover of the light-harvesting chlorophyll a/b-protein in Lemna gibba grown with intermittent red light: possible translational control
Synthesis and turnover of the light-harvesting chlorophyll a/b-protein in Lemna gibba grown with intermittent red light: possible translational control

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Synthesis and turnover of the light-harvesting chlorophyll a/b-protein in Lemna gibba grown with intermittent red light: possible translational control
Synthesis and turnover of the light-harvesting chlorophyll a/b-protein in Lemna gibba grown with intermittent red light: possible translational control
Journal Article

Synthesis and turnover of the light-harvesting chlorophyll a/b-protein in Lemna gibba grown with intermittent red light: possible translational control

1982
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Overview
Lemna gibba L. G-3 plants grown heterotrophically in the dark with intermittent red light (2 min every 8 h) contain a substantial amount of translatable mRNA encoding the light-harvesting chlorophyll (Chl) a/b-protein. However, very little [35S]methionine is incorporated into the apoproteins during a 1-h labeling period in the dark in these plants compared to plants grown in continuous white light. The Chl a/b-protein mRNA is found to be associated with functioning polysomes in plants grown in the dark with intermittent red illumination (R plants). The small amounts of the apoproteins which are synthesized by these plants are found in the membrane fraction; neither the mature apoproteins nor their precursor(s) can be detected immunologically in the soluble fraction. The protein does not accumulate in these plants. Pulse-chase experiments with the R plants demonstrate that the newly synthesized apoproteins have a half-life of about 10 h in the dark. This turnover is not sufficient to explain the observed 20-fold difference in [35S]methionine incorporation into the apoprotein between white-light-grown and R plants. We therefore suggest that the synthesis of the Chl a/b-apoproteins can be regulated by a light-dependent step at the level of translation, and that this regulation occurs after the initiation of translation.