Ribulose-1,5-bisphosphate carboxylase (RuBPCase) was purified from the marine chromophyte Olisthodiscus luteus. This study represents the first extensive analysis of RuBPCase from a chromophytic plant species as well as from an organism where both subunits of the enzyme are encoded on the chloroplast genome. The size of the purified holoenzyme (17.9 Svedberg units, 588 Although all chlorophytes code for the LS and SS of this enzyme in the nucleus and chloroplast, respectively (11,30), in the chromophytic alga Olisthodiscus luteus, immunoprecipitation of protein products synthesized in the presence of the cytoplasmic ribosome inhibitor cycloheximide gives evidence that both subunits of RuBPCase are synthesized in the chloroplast (20). Expression of the LS and SS polypeptides in a linked transcription-translation system using a cloned 0. luteus ctDNA fragment demonstrates (20) definitively that both genes are encoded on the plastid genome. The rbcL and rbcS genes are present on a large 20 kb inverted repeat which also contains psbA and ribosomal RNA cistrons (20) (TP Delaney, RA Cattolico, unpublished data). To date, except in Chlamydomonas eugametos (10) and Pelargonium (17) where the rbcL gene is also present on an inverted repeat, the large subunit of RuBPCase is present in single copy on every chloroplast genome analyzed. Gene arrangement of rbcL and rbcS in the eukaryote 0. luteus appears to be similar to that observed in cyanelles (permanent blue-green algallike symbionts which are present in a diverse array of colorless host cells) and blue-green algae. The close proximity of rbcL and rbcS in 0. luteus suggests that both these genes may be under the control of a single promotor as seen in prokaryotes and cyanelles (16,25).It would be of interest to know how the chloroplast DNA