title: Interruption of the Calvin cycle inhibits the repair of Photosystem II from photodamage.
abstract: In photosynthetic organisms, impairment of the activities of enzymes in the Calvin cycle enhances the extent of photoinactivation of Photosystem II (PSII). We investigated the molecular mechanism responsible for this phenomenon in the unicellular green alga Chlamydomonas reinhardtii. When the Calvin cycle was interrupted by glycolaldehyde, which is known to inhibit phosphoribulokinase, the extent of photoinactivation of PSII was enhanced. The effect of glycolaldehyde was very similar to that of chloramphenicol, which inhibits protein synthesis de novo in chloroplasts. The interruption of the Calvin cycle by the introduction of a missense mutation into the gene for the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) also enhanced the extent of photoinactivation of PSII. In such mutant 10-6C cells, neither glycolaldehyde nor chloramphenicol has any additional effect on photoinactivation. When wild-type cells were incubated under weak light after photodamage to PSII, the activity of PSII recovered gradually and reached a level close to the initial level. However, recovery was inhibited in wild-type cells by glycolaldehyde and was also inhibited in 10-6C cells. Radioactive labelling and Northern blotting demonstrated that the interruption of the Calvin cycle suppressed the synthesis de novo of chloroplast proteins, such as the D1 and D2 proteins, but did not affect the levels of psbA and psbD mRNAs. Our results suggest that the photoinactivation of PSII that is associated with the interruption of the Calvin cycle is attributable primarily to the inhibition of the protein synthesis-dependent repair of PSII at the level of translation in chloroplasts.
authors.affiliation: Division of Cellular Regulation, National Institute for Basic Biology, Myodaiji, Okazaki 444-8585, Japan.
authors.forename: Shunichi
authors.initials: S
authors.lastname: Takahashi
authors.forename: Norio
authors.initials: N
authors.lastname: Murata
mesh_terms: D000079:Acetaldehyde / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D000818:Animals; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism; D016825:Chlamydomonas reinhardtii / Q000502:physiology*; D004579:Electron Transport; D004791:Enzyme Inhibitors / Q000494:pharmacology; D008027:Light; D020125:Mutation, Missense; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000037:antagonists & inhibitors / Q000378:metabolism; D010788:Photosynthesis / Q000502:physiology*; D045332:Photosystem II Protein Complex / Q000235:genetics / Q000378:metabolism*; D015800:Protozoan Proteins / Q000096:biosynthesis; D012273:Ribulose-Bisphosphate Carboxylase / Q000235:genetics / Q000378:metabolism
chemical_list: D029681:Arabidopsis Proteins; D004791:Enzyme Inhibitors; D045332:Photosystem II Protein Complex; D015800:Protozoan Proteins; C479885:PsbD protein, Arabidopsis; C422369:photosystem II, psbA subunit; D017853:Phosphotransferases (Alcohol Group Acceptor); C022390:phosphoribulokinase; D012273:Ribulose-Bisphosphate Carboxylase; D000079:Acetaldehyde; C010972:glycolaldehyde