title: Arabidopsis thaliana plants lacking the PSI-D subunit of photosystem I suffer severe photoinhibition, have unstable photosystem I complexes, and altered redox homeostasis in the chloroplast stroma.
abstract: The PSI-D subunit of photosystem I is a hydrophilic subunit of about 18 kDa, which is exposed to the stroma and has an important function in the docking of ferredoxin to photosystem I. We have used an antisense approach to obtain Arabidopsis thaliana plants with only 5-60% of PSI-D. No plants were recovered completely lacking PSI-D, suggesting that PSI-D is essential for a functional PSI in plants. Plants with reduced amounts of PSI-D showed a similar decrease in all other subunits of PSI including the light harvesting complex, suggesting that in the absence of PSI-D, PSI cannot be properly assembled and becomes degraded. Plants with reduced amounts of PSI-D became light-stressed even in low light although they exhibited high non-photochemical quenching (NPQ). The high NPQ was generated by upregulating the level of violaxanthin de-epoxidase and PsbS, which are both essential components of NPQ. Interestingly, the lack of PSI-D affected the redox state of thioredoxin. During the normal light cycle thioredoxin became increasingly oxidized, which was observed as decreasing malate dehydrogenase activity over a 4-h light period. This result shows that photosynthesis was close to normal the first 15 min, but after 2-4 h photoinhibition dominated as the stroma progressively became less reduced. The change in the thiol disulfide redox state might be fatal for the PSI-D-less plants, because reduction of thioredoxin is one of the main switches for the initiation of CO2 assimilation and photoprotection upon light exposure.
authors.affiliation: Plant Biochemistry Laboratory, Department of Plant Biology, The Royal Veterinary and Agricultural University, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark. anna@kvl.dk
authors.forename: Anna
authors.initials: A
authors.lastname: Haldrup
authors.forename: Christina
authors.initials: C
authors.lastname: Lunde
authors.forename: Henrik Vibe
authors.initials: HV
authors.lastname: Scheller
mesh_terms: D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics* / Q000502:physiology*; D002734:Chlorophyll / Q000737:chemistry / Q000378:metabolism; D002736:Chloroplasts / Q000378:metabolism; D015536:Down-Regulation; D005822:Genetic Vectors; D015151:Immunoblotting; D008027:Light; D045342:Light-Harvesting Protein Complexes; D008291:Malate Dehydrogenase / Q000378:metabolism; D050538:Malate Dehydrogenase (NADP+); D008969:Molecular Sequence Data; D016376:Oligonucleotides, Antisense / Q000494:pharmacology; D010084:Oxidation-Reduction; D010641:Phenotype; D045322:Photosynthetic Reaction Center Complex Proteins / Q000235:genetics*; D045331:Photosystem I Protein Complex; D010940:Plant Proteins; D030821:Plants, Genetically Modified; D017386:Sequence Homology, Amino Acid; D013050:Spectrometry, Fluorescence; D013696:Temperature; D013879:Thioredoxins / Q000378:metabolism; D013997:Time Factors
chemical_list: D045342:Light-Harvesting Protein Complexes; D016376:Oligonucleotides, Antisense; D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex; D010940:Plant Proteins; D002734:Chlorophyll; D013879:Thioredoxins; D008291:Malate Dehydrogenase; D050538:Malate Dehydrogenase (NADP+)