pheophytin-a and magnesium-protoporphyrin

Low Chlorophyll Accumulation A (LCAA) antisense plants were obtained from a screen for genes whose partial down-regulation results in a strong chlorophyll deficiency in tobacco (Nicotiana tabacum). The LCAA mutants are affected in a plastid-localized protein of unknown function, which is conserved in cyanobacteria and all photosynthetic eukaryotes. They suffer from drastically reduced light-harvesting complex (LHC) contents, while the accumulation of all other photosynthetic complexes per leaf area is less affected. As the disturbed accumulation of LHC proteins could be either attributable to a defect in LHC biogenesis itself or to a bottleneck in chlorophyll biosynthesis, chlorophyll synthesis rates and chlorophyll synthesis intermediates were measured. LCAA antisense plants accumulate magnesium (Mg) protoporphyrin monomethylester and contain reduced protochlorophyllide levels and a reduced content of CHL27, a subunit of the Mg protoporphyrin monomethylester cyclase. Bimolecular fluorescence complementation assays confirm a direct interaction between LCAA and CHL27. 5-Aminolevulinic acid synthesis rates are increased and correlate with an increased content of glutamyl-transfer RNA reductase. We suggest that LCAA encodes an additional subunit of the Mg protoporphyrin monomethylester cyclase, is required for the stability of CHL27, and contributes to feedback-control of 5-aminolevulinic acid biosynthesis, the rate-limiting step of chlorophyll biosynthesis.

Topics: Amino Acid Sequence; Aminolevulinic Acid; Chlorophyll; Chlorophyll A; Conserved Sequence; Evolution, Molecular; Feedback, Physiological; Fluorescence; Gene Expression Regulation, Plant; Intramolecular Oxidoreductases; Light-Harvesting Protein Complexes; Molecular Sequence Data; Nicotiana; Oxidation-Reduction; Phenotype; Photosynthesis; Plant Proteins; Plastids; Protein Transport; Protoporphyrins; RNA, Antisense; Sequence Alignment; Tetrapyrroles