Distribution of the major light-harvesting chlorophyll a/b-protein (LHCII) and its mRNA within bundle sheath and mesophyll cells of maize (Zea mays L.) was studied using in situ immunolocalization and hybridization, respectively. In situ hybridization with specific LHCII RNA probes from maize and Lemna gibba definitively shows the presence of high levels of mRNA for LHCII in both bundle sheath cells and mesophyll cells. In situ immunolocalization studies, using an LHCII monoclonal antibody, demonstrate the presence of LHCII polypeptides in chloroplasts of both cell types. The polypeptide composition of LHCII and the amount of LHCII in bundle sheath cells are different from those in mesophyll cells. Both mesophyll and bundle sheath chloroplasts can take up, import and process the in vitro transcribed and translated LHCII precursor protein from L. gibba. Although bundle sheath chloroplasts incorporate LHCII into the pigmented light-harvesting complex, the efficiency is lower than that in mesophyll chloroplasts.Leaves of C4 plants contain two distinct types of photosynthetic cells, mesophyll (M3) and bundle sheath (BS), that are quite distinctly organized both structurally and functionally. Since the discovery of C4-dicarboxylic acid photosynthesis, much effort has been directed to determining the sequence of reactions in that pathway (3,11,20,26,28,29). Accumulated data agree upon the existence in C4 plants of an active PSI in both cell types and of PSII in M cells; however, there is disagreement about the existence of PSII activity in BS cells of maize and even about the presence of some of the constituents of PSII in BS cells (2,3,10,20,26,28,29 (3,26,28). In all of these studies, BS cells were first separated from M cells and then examined for the presence of mRNA for LHCII, or for the polypeptide itself.The apoproteins of LHCII are encoded by a nuclear gene family and synthesized on cytoplasmic ribosomes as a watersoluble, higher mol wt precursor form(s), preLHCII. During its insertion into the thylakoid membranes it is processed to its mature, water-insoluble form, and photosynthetic pigments are added to it (7,14,24,25,30). The sequence of events that leads to its incorporation into the LHCII complex is, however, largely unknown. Uptake experiments in which in vitro synthesized preLHCII is incubated with a suspension of intact chloroplasts show that the efficiency with which the preLHCII is processed to its mature size and incorporated into the pigmented LHCII complex depends upon the stage of plastid development (5). Import ofthe precursor by plastids is energy dependent and requires a putative receptor in the chloroplast envelope (9,13,16). A stromal factor(s), probably proteinaceous, is required for insertion into the thylakoid membrane (5,8).In the present study we show qualitatively, using in situ hybridization and in situ immunolocalization techniques which avoid fractionation of the two cell types, that mRNA for LHCII and the LHCII gene translation product(s) accumulate to a detectable level i...