Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1767, Issue 6, Pages 820-828Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2006.11.016
Keywords
photosystem II; D1-protein; D2-protein; FtsH protease; UV-B damage
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Funding
- BBSRC [BB/E006388/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/E006388/1] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [BB/E006388/1] Funding Source: Medline
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The photosystem two (PSII) complex found in oxygenic photosynthetic organisms is susceptible to damage by UV-B irradiation and undergoes repair in vivo to maintain activity. Until now there has been little information on the identity of the enzymes involved in repair. In the present study we have investigated the involvement of the FtsH and Deg protease families in the degradation of UV-B-damaged PSII reaction center subunits, D1 and D2, in the cyanobacterium Synechocystis 6803. PSII activity in a Delta FtsH (slr0228) strain, with an inactivated slr0228 gene, showed increased sensitivity to UV-B radiation and impaired recovery of activity in visible light after UV-B exposure. In contrast, in Delta Deg-G cells, in which all the three deg genes were inactivated, the damage and recovery kinetics were the same as in the WT. Immunoblotting showed that the loss of both the D1 and D2 proteins was retarded in A FtsH (slr0228) during UV-B exposure, and the extent of their restoration during the recovery period was decreased relative to the WT. However, in the Delta Deg-G cells the damage and recovery kinetics of D1 and D2 were the same as in the WT. These data demonstrate a key role of FtsH (slr0228), but not the Deg proteases, for the repair of PSII during and following UV-B radiation at the step of degrading both of the UV-B damaged D1 and D2 reaction center subunits. (c) 2006 Elsevier B.V. All rights reserved.
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