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-ah-binding protein. Steady-state concentrations of mRNA for the small subunit of ribulose-l,5-bisphosphate carboxylase were hardly affected under all investigated light intensities.The process of thylakoid formation has been thoroughly investigated and although the principle mechanisms are understood the complete details are not yet known [l]. This is especially true for the various mechanisms which precisely regulate photosynthetic efficiency and which have to take place under natural conditions e.g. adaptation to low-light and high-light intensities and also low and high temperatures. During the process of greening, the coordinated expression of genes has been observed [2]. Among the proteins that appear first during greening are early light-inducible proteins (ELIP). These nuclear-encoded thylakoid-membrane proteins share homology with the apoprotein of the chlorophyll-albbinding protein (LHC 11) [3-51 and with the recently discovered 22-kDa protein of photosystem I1 (psbS) [6, 71. The latter similarity seems important as, in contrast to LHC, the binding of pigments has not been detected for ELIP or psbS.During the last two years, ELIP have been recognized as light-stress proteins [8 -101. These studies, derived from earlier findings, showed that after transport into mature chloroplasts ELIP are found in the vicinity of photosystem I1 and can be crosslinked to the D1 protein [ll]. Since D1 is known to rapidly turn over during high-light stress or photoinhibi- tion [12, 131, the expression of ELIP was studied under conditions of light stress. It was found th...