Summary
Cyanophora paradoxa is an important model organism for the study of the transition from endocytobiontic cyanobacteria to factual eukaryotic cell organelles. The cyanelles of these organisms possess cyanobacterial, as well as plastidic, characteristics. Although the transfer of cyanellar proteins from cytosolic into cyanellar space has been shown, the process of translocation of a known protein across the peptidoglycan layer and the envelope membranes has not been characterized. In this study we demonstrate that a specific and obligate cyanelle protein —Ferredoxin-NADP+-oxidoreductase (FNR) — is coded on the nuclear genome, synthesized on 80S ribosomes and transported from the eukaryotic cell compartment into the cyanelles of Cyanophora paradoxa, an original intracellular host-guest relation. These results indicate a gene transfer from guest to host genome and support the view that, in spite of their cyanobacterial origin, cyanelles have been evolved to cell organelles comparable to plastids.
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Communicated by K. Wolf
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Bayer, M.G., Maier, T.L., Gebhart, U.B. et al. Cyanellar Ferredoxin-NADP+-oxidoreductase of Cyanophora paradoxa is encoded by the nuclear genome and synthesized on cytoplasmatic 80S ribosomes. Curr Genet 17, 265–267 (1990). https://doi.org/10.1007/BF00312619
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DOI: https://doi.org/10.1007/BF00312619