The role of carbonic anhydrase α-CA4 in the adaptive reactions of photosynthetic apparatus: the study with α-CA4 knockout plants

• Published in: Protoplasma 2020-03, Vol.257 (2), p.489-499
• Main Authors: Rudenko, Natalia N., Fedorchuk, Tatyana P., Terentyev, Vasily V., Dymova, Olga V., Naydov, Ilya A., Golovko, Tamara K., Borisova-Mubarakshina, Maria M., Ivanov, Boris N.
• Format: Article
• Language: English
• Subjects: Biomedical and Life Sciences; Carbonic anhydrases; Cell Biology; Chlorophyll; Core protein; D1 protein; Electron transport; Life Sciences; Mutants; Original Article; Photosynthetic apparatus; Photosystem I; Photosystem II; Pigments; Plant Sciences; Proteins; Thylakoid membranes; Thylakoids; Violaxanthin; Zoology
• ISSN: 0033-183X; 1615-6102
• DOI: 10.1007/s00709-019-01456-1

The role of α-carbonic anhydrase 4 (α-CA4) in photosynthetic machinery functioning in thylakoid membranes was studied, using Arabidopsis thaliana wild type plants (WT) and the plants with knockout of At4g20990 gene encoding α-CA4 (αCA4-mut) grown both in low light (LL, 80 μmol quanta m −2 s −1 ) or in high light (HL, 400 μmol quanta m −2 s −1 ). It was found that a content of PsbS protein, one of determinants of non-photochemical quenching of chlorophyll fluorescence, increased in mutants by 30% and 100% compared with WT plants in LL and in HL, respectively. Violaxanthin cycle pigments content and violaxanthin deepoxidase activity in HL were also higher in αCA4-mut than in WT plants. The content of PSII core protein, D1, when adapting to HL, decreased in WT plants and remained unchanged in mutants. This indicates, that the decrease in the content of Lhcb1 and Lhcb2 proteins in HL (Rudenko et al. Protoplasma 55(1):69-78, 2018) in WT plants resulted from decrease of both Photosystem II (PSII) complex content and content of these proteins in this complex, whereas in αCA4-mut plants from the latter process only. The absence of α-CA4 did not affect the rate of electron transport through Photosystem I (PSI) in thylakoids of mutant vs. WT, but led to 50–80% increase in the rate of electron transport from H 2 O to Q A , evidencing the location of α-CA4 close to PSII. The latter difference may raise the question about its causal connection with the difference in the D1 protein content change during adapting to increased illumination in the presence and the absence of α-CA4.