Characterization of a chloroplast mutation in the psaA2 gene of Chlamydomonas reinhardtii.
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.
Girard-Bascou
J
J
Institut de Biologie Physico-Chimique, Paris, France.
Choquet
Y
Y
Schneider
M
M
Delosme
M
M
Dron
M
M
D000595:Amino Acid Sequence; D001483:Base Sequence; D002696:Chlamydomonas / Q000235:genetics* / Q000378:metabolism; D002734:Chlorophyll / Q000235:genetics*; D002736:Chloroplasts / Q000378:metabolism*; D004262:DNA Restriction Enzymes; D005796:Genes; D045342:Light-Harvesting Protein Complexes; D008969:Molecular Sequence Data; D009154:Mutation; D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex; D010940:Plant Proteins / Q000235:genetics*
D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex; D010940:Plant Proteins; D002734:Chlorophyll; D004262:DNA Restriction Enzymes