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Accelerated Degradation of the D2 Protein of Photosystem II Under Ultraviolet Radiation
Author(s) -
Jansen Marcel A. K.,
Greenberg Bruce M.,
Edelman Marvin,
Mattoo Autar K.,
Gaba Victor
Publication year - 1996
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1996.tb09636.x
Subject(s) - photosystem ii , degradation (telecommunications) , photosynthesis , photosystem i , biophysics , photochemistry , protein degradation , chemistry , photosystem , biology , biochemistry , telecommunications , computer science
The D2 protein of photosystem II is relatively stable in vivo under photosynthetic active radiation, but its degradation accelerates under UVB radiation. Little is known about accelerated D2 protein degradation. We characterized wavelength dependence and sensitivity toward photosystem II inhibitors. The in vivo D2 degradation spectrum resembles the pattern for the rapidly turning over D1 protein of photosystem II, with rates being maximal in the UVB region. We propose that D2 degradation, like D1 degradation, is activated by distinct photosensitizers in the UVB and visible regions of the spectrum. In both wavelength regions, photosystem II inhibitors that are known to be targeted to the D1 protein affect D2 degradation. This suggests that degradation of the two proteins is coupled, D2 degradation being influenced by events occurring at the Q B niche on the D1 protein.