Synechocystis 6803 mutants expressing distinct forms of the Photosystem II D1 protein from Synechococcus 7942: relationship between the psbA coding region and sensitivity to visible and UV-B radiation
Language English Country Netherlands Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12907301
DOI
10.1016/s0005-2728(03)00064-1
PII: S0005272803000641
Knihovny.cz E-resources
- MeSH
- Phenotype MeSH
- Photosynthetic Reaction Center Complex Proteins genetics metabolism radiation effects MeSH
- Photosystem II Protein Complex * MeSH
- Mutation MeSH
- Cyanobacteria genetics metabolism radiation effects MeSH
- Light MeSH
- Ultraviolet Rays MeSH
- Structure-Activity Relationship MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Photosynthetic Reaction Center Complex Proteins MeSH
- Photosystem II Protein Complex * MeSH
- photosystem II, psbA subunit MeSH Browser
Synechocystis PCC 6803 mutants expressing either the "low light" (D1:1) or the "high light" (D1:2) form of the Photosystem II (PSII) D1 protein from Synechococcus PCC 7942 were constructed and characterized with respect to properties of PSII and sensitivity to visible and UV-B radiation. The AI and AIII mutants (containing only the D1:1 and D1:2 forms, respectively) exhibited very similar PSII characteristics as the control strain and they differed only in the accelerated decay kinetics of flash-induced variable fluorescence measured in the presence of DCMU. However, the mutants showed increased sensitivity to photodamage induced by visible and UV-B radiation, with higher loss of PSII activity in the AI than in the AIII strain. Thus, the difference between strains containing D1:1 and D1:2 found previously in Synechococcus 7942 is maintained after transfer of corresponding psbA genes into Synechocystis 6803 and is directly related to the coding region of these genes. The higher light sensitivity of the AI mutant is caused partly by the higher rate of photodamage and partly by the less efficient PSII repair.
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