A plastome mutation affects processing of both chloroplast and nuclear DNA-encoded plastid proteins.
Immunoblotting of a chloroplast mutant (pm7) of Oenothera showed that three proteins, cytochrome f and the 23 kDa and 16 kDa subunits of the oxygen-evolving subcomplex of photosystem II, were larger than the corresponding mature proteins of the wild type and, thus, appear to be improperly processed in pm7. The mutant is also chlorotic and has little or no internal membrane development in the plastids. The improperly processed proteins, and other proteins that are completely missing, represent products of both the plastid and nuclear genomes. To test for linkage of these defects, a green revertant of pm7 was isolated from cultures in which the mutant plastids were maintained in a nuclear background homozygous for the plastome mutator (pm) gene. In this revertant, all proteins analyzed co-reverted to the wild-type condition, indicating that a single mutation in a plastome gene is responsible for the complex phenotype of pm7. These results suggest that the defect in pm7 lies in a gene that affects a processing protease encoded in the chloroplast genome.
Johnson
E M
EM
Department of Botany and Plant Pathology, Michigan State University, East Lansing 48824.
Schnabelrauch
L S
LS
Sears
B B
BB
D000595:Amino Acid Sequence; D002467:Cell Nucleus / Q000378:metabolism*; D002736:Chloroplasts / Q000378:metabolism*; D004247:DNA / Q000235:genetics / Q000378:metabolism; D008040:Genetic Linkage; D015151:Immunoblotting; D008969:Molecular Sequence Data; D009154:Mutation; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000235:genetics*; D011499:Protein Processing, Post-Translational; D016415:Sequence Alignment
D010940:Plant Proteins; D004247:DNA