R. Barbato et al., Effects of ultraviolet-B light on photosystem II phosphoproteins in barleywild type and its chlorophyll b-less mutant chlorina f2, J PHOTOCH B, 48(2-3), 1999, pp. 189-193
Citations number
27
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
The effects of ultraviolet-B light on the level and steady-state phosphoryl
ation of photosystem II proteins have been studied in barley wild type and
its chlorophyll b-less mutant chlorina f2. In the wild type, ultraviolet-B
radiation is found to promote dephosphorylation of all thylakoid phosphopro
teins. In addition, for reaction-centre proteins D1 and D2, dephosphorylati
on is paralleled by degradation. Photosystem II core proteins in the mutant
are not found to be significantly phosphorylated in any experimental condi
tions, and loss of D1 and D2 reaction-centre proteins is slightly faster th
an in the wild type. These results are consistent with the possibility that
phosphorylation of reaction-centre proteins affects their stability, possi
bly by slowing down the rate of degradation, as in the case of visible ligh
t [E. Rintamaki, R. Kettunen, E.-M. Aro, J. Biol. Chem. 271 (1996) 14870-14
875]. (C) 1999 Elsevier Science S.A. All rights reserved.