Chloroplast development involves the nucleus, the cytoplasm and the chloroplast of plant cells. This may be illustrated by reference to the two most abundant proteins of the chloroplast: (i) the soluble CO$_2$-fixing enzyme ribulose 1,5-bisphosphate carboxylase-oxygenase, whose large subunit (LSU) is encoded in chloroplast DNA and synthesized on chloroplast ribosomes and whose small subunit (SSU) is encoded in nuclear DNA, synthesized on cytoplasmic ribosomes in precursor form and transported into chloroplasts, and (ii) the thylakoid-bound light-harvesting chlorophyll a/b complex, whose pigment components are synthesized in the chloroplast and whose apoproteins resemble the SSU in site of coding and site of synthesis. We have examined the extent to which biosynthetic events in the nucleocytoplasmic compartments are coordinated with those inside the chloroplast during the de-etiolation of pea seedlings. We have examined the levels of LSU, SSU and the light-harvesting chlorophyll a/b protein (LHCP) by using a highly specific radioimmune assay. The steady-state levels of the corresponding mRNAs have been determined using specific cloned DNA probes. With the SSU, the mRNA and protein levels are near the limit of detection in dark-grown plants but increase markedly under continuous white light, with a lag of about 24 h. The protein appears to be under simple phytochrome control at the level of the steady-state concentration of its mRNA. The LSU also appears to be regulated through the steady-state concentration of its mRNA but in this case the mRNA is not under simple phytochrome control. The LHCP mRNA is readily detectable in dark-grown plants and accumulates further under illumination in a phytochrome-mediated manner. However, the LHCP itself (like chlorophyll) is not detectable in dark-grown plants and accumulates to high levels only under continuous illumination, with a lag of about 6 h. Post-translational control is particularly important in the accumulation of the LHCP: continuous chlorophyll synthesis is required for the stabilization of the protein within the thylakoid membrane, at least during the early stages of chloroplast development.