Expression of a highly active catalase VktA in the cyanobacterium Synechococcus elongatus PCC 7942 alleviates the photoinhibition of photosystem II

• Published in: Photosynthesis research Vol. 117; no. 1-3; pp. 509 - 515
• Main Authors: Jimbo, Haruhiko, Noda, Akiko, Hayashi, Hidenori, Nagano, Takanori, Yumoto, Isao, Orikasa, Yoshitake, Okuyama, Hidetoshi, Nishiyama, Yoshitaka
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer-Verlag 01.11.2013; Springer Netherlands; Springer; Springer Nature B.V
• Subjects: Bacteria; Bacterial Proteins - metabolism; Biochemistry; Biomedical and Life Sciences; catalase; Catalase - metabolism; chloramphenicol; Cyanobacteria; D1 protein; Enzymes; Gene expression; Genes, Bacterial - genetics; hydrogen peroxide; Hydrogen Peroxide - pharmacology; Life Sciences; Oxidative stress; Photochemical Processes - drug effects; photoinhibition; Photosynthesis; photosystem II; Photosystem II Protein Complex - metabolism; Plant Genetics and Genomics; Plant Physiology; Plant Sciences; Protein biosynthesis; Protein synthesis; psychrophilic bacteria; Regular Paper; Synechococcus - drug effects; Synechococcus - enzymology; Synechococcus - genetics; Synechococcus elongatus; Synechococcus sp. PCC 7942; temperature; Vibrio - enzymology; Vibrio - genetics; Vibrio rumoiensis; Photoinhibition; Oxidative stress; Photosystem II; Catalase; Protein synthesis
• ISSN: 0166-8595; 1573-5079
• DOI: 10.1007/s11120-013-9804-7

The repair of photosystem II (PSII) after photodamage is particularly sensitive to reactive oxygen species—such as H₂O₂, which is abundantly produced during the photoinhibition of PSII. In the present study, we generated a transformant of the cyanobacterium Synechococcus elongatus PCC 7942 that expressed a highly active catalase, VktA, which is derived from a facultatively psychrophilic bacterium Vibrio rumoiensis, and examined the effect of expression of VktA on the photoinhibition of PSII. The activity of PSII in transformed cells declined much more slowly than in wild-type cells when cells were exposed to strong light in the presence of H₂O₂. However, the rate of photodamage to PSII, as monitored in the presence of chloramphenicol, was the same in the two lines of cells, suggesting that the repair of PSII was protected by the expression of VktA. The de novo synthesis of the D1 protein, which is required for the repair of PSII, was activated in transformed cells under the same stress conditions. Similar protection of the repair of PSII in transformed cells was also observed under strong light at a relatively low temperature. Thus, the expression of the highly active catalase mitigates photoinhibition of PSII by protecting protein synthesis against damage by H₂O₂ with subsequent enhancement of the repair of PSII.