Effects of light stress on the expression of early light-inducible proteins in barley

Treatment of six-day-old barley leaves with white light of high intensity, 250-2000 W/m2, leads to a linear increase in the steady-state concentrations of early light-inducible protein (ELIP) mRNA followed by an accumulation of the protein. Accumulation of ELIP mRNA, under light stress, is highest i...

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Veröffentlicht in:European journal of biochemistry 1993-06, Vol.214 (3), p.779-786
Hauptverfasser: Potter, E, Kloppstech, K
Format: Artikel
Sprache:eng
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Zusammenfassung:Treatment of six-day-old barley leaves with white light of high intensity, 250-2000 W/m2, leads to a linear increase in the steady-state concentrations of early light-inducible protein (ELIP) mRNA followed by an accumulation of the protein. Accumulation of ELIP mRNA, under light stress, is highest in the basal third of the leaf and declines to approximately 50% of this level in the apical segment. The amount of the accumulated protein decreases more steeply towards the tip than would be expected from mRNA levels. This finding, as well as the fact that during greening a massive accumulation of the protein starts only at a time when the steady-state concentrations of ELIP mRNA have declined to 10% of the maximal value, indicate post-transcriptional control. Accumulation is presumably achieved by stabilization of the protein. ELIP mRNA and protein levels, induced by a 2-h period of high-light stress, are lowest in the afternoon and highest at midnight and during the morning. The inducibility of ELIP by high light is therefore under diurnal control. An increase of light stress, due to application of the carotenoid-biosynthesis inhibitor norfluorazon, results in a considerable induction of ELIP mRNA and protein. The plant hormone abscisic acid exerts only a small effect on the mRNA level. In all cases studied, the light-induced increase in the amount of ELIP mRNA was accompanied by a corresponding decline in the mRNA levels for the apoprotein of the chlorophyll-a/b-binding protein. Steady-state concentrations of mRNA for the small subunit of ribulose-1,5-bisphosphate carboxylase were hardly affected under all investigated light intensities.
ISSN:0014-2956
1432-1033
DOI:10.1111/j.1432-1033.1993.tb17980.x