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Characterization of a chloroplast mutation in the psaA2 gene of Chlamydomonas reinhardtii |
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| Authors: | Jacqueline Girard-Bascoul Yves Choquet Michel Schneider Monique Delosmel Michel Dron |
| Affiliation: | (1) Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, F-75005 Paris, France;(2) Laboratoire de Biologie Moléculaire Végétale, Université de Paris Sud, F-91405 Orsay, France;(3) Present address: Déparement de Biologie Moldculaire, Université de Genéve, Sciences II, 30 quai Ernst Ansermet, CH-1211 Genéve 4, Suisse;(4) Present address: Department of Biology, University of California, 92109 San Diego, CA, USA;(5) Present address: The Salk Institute, 85800 San Diego, CA, USA |
| Abstract: | Summary The synthesis of polypeptides related to the CPI chlorophyll-protein complex of photosystem I has been studied by pulse-labeling experiments in twenty chloroplast mutants of Chlamydomonas reinhardtii. Three mutations of the same locus (Girard-Bascou 1987) result in the absence of these CPI-related polypeptides. Among these mutations one, (FUD26) leads to the synthesis of a new polypeptide presumed to be a truncated CPI apoprotein. The molecular characterization of this mutation in the psaA2 gene has been achieved by DNA sequencing the 3 end of this gene. The FUD26 mutation is a 4 base pair deletion resulting in frameshift and premature termination of the protein. |
| Keywords: | Chlamydomonas reinhardtii Photosystem I mutants CPI apoproteins psaA2 gene |
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