The light-induced greening of etiolated barley plants is used as a model to study the light-dependent control of plastid development. Upon illumination a rapid transformation of etioplasts to chloroplasts is induced. The effect of illumination does not only include the light-dependent chlorophyll synthesis but also the appearance or decline of specific proteins within the plastid membrane fractions. So far two of these proteins have been studied in detail. The light-harvesting chlorophyll a/b protein (LHCP) is one of the major protein constituents of the thylakoid membrane of chloroplasts. However, this protein is not detectable among the membrane polypeptides of etioplasts. Illumination of dark-grown barley plants induces a massive insertion of the LHCP. The appearance of the protein is controlled by the cooperation of at least two distinct photoreceptors: protochlorophyllide and phytochrome. In dark-grown barley plants not only the LHCP but also its mRNA is not detectable. The light-dependent appearance of mRNA activity for the LHCP is under the control of phytochrome (Pfr). Even though the appearance of mRNA activity is induced via Pfr by a single red light pulse, the assembly of the complete LHCP takes place only under continuous illumination, which allows chlorophyll synthesis. The second protein analyzed so far is the NADPH-protochlorophyllide-oxidoreductase. This enzyme catalyzes the light-dependent reduction of protochlorophyllide to chlorophyllide and thus controls one of the first detectable light-dependent reactions during the greening period. It is generally assumed that this enzyme is responsible for the overall chlorophyll synthesis and accumulation during the greening period.(ABSTRACT TRUNCATED AT 250 WORDS)