Light-Adaptation of Photosystem II Is Mediated by the Plastoquinone Pool†

Biochemistry ◽  
2003 ◽  
Vol 42 (25) ◽  
pp. 7655-7662 ◽  
Author(s):  
Karin A. Åhrling ◽  
Sindra Peterson
2015 ◽  
Vol 112 (5) ◽  
pp. 1613-1618 ◽  
Author(s):  
Xin Hou ◽  
Aigen Fu ◽  
Veder J. Garcia ◽  
Bob B. Buchanan ◽  
Sheng Luan

In earlier studies we have identified FKBP20-2 and CYP38 as soluble proteins of the chloroplast thylakoid lumen that are required for the formation of photosystem II supercomplexes (PSII SCs). Subsequent work has identified another potential candidate functional in SC formation (PSB27). We have followed up on this possibility and isolated mutants defective in the PSB27 gene. In addition to lack of PSII SCs, mutant plants were severely stunted when cultivated with light of variable intensity. The stunted growth was associated with lower PSII efficiency and defective starch accumulation. In response to high light exposure, the mutant plants also displayed enhanced ROS production, leading to decreased biosynthesis of anthocyanin. Unexpectedly, we detected a second defect in the mutant, namely in CP26, an antenna protein known to be required for the formation of PSII SCs that has been linked to state transitions. Lack of PSII SCs was found to be independent of PSB27, but was due to a mutation in the previously described cp26 gene that we found had no effect on light adaptation. The present results suggest that PSII SCs, despite being required for state transitions, are not associated with acclimation to changing light intensity. Our results are consistent with the conclusion that PSB27 plays an essential role in enabling plants to adapt to fluctuating light intensity through a mechanism distinct from photosystem II supercomplexes and state transitions.


1983 ◽  
Vol 38 (9-10) ◽  
pp. 793-798 ◽  
Author(s):  
W. S. Cohen ◽  
J. R. Barton

Photosystem II particles that retain the ability to evolve O2 have been used to examine acceptor and inhibitor sites in the photosynthetic electron transfer chain between Q and plastoquinone. Employing the water to dichlorobenzoquinone reaction to assay photosystem II activity, we have demonstrated that electron transport in thylakoids and particles is equally sensitive to inhibition by DCMU. dinoseb, metribuzin, HQNO and DBMIB. Based on differential sensitivity to inhibition by DCMU vs. HQNO or DBMIB, we suggest that when synthetic quinones, e.g. 2,6-dichlorobenzoquinone operate as Hill reagents in particles they are reduced primarily by the plastoquinone pool. When synthetic quinones, e.g. 5,6-methylenedioxy-2,3-dimethyl benzoquinone act as autoxidizable acceptors they accept electron from the Q/B complex at a point that is located between the DCMU and HQNO (DBMIB) inhibition sites.


2016 ◽  
Vol 81 (8) ◽  
pp. 858-870
Author(s):  
O. V. Voloshina ◽  
Y. V. Bolychevtseva ◽  
F. I. Kuzminov ◽  
M. Y. Gorbunov ◽  
I. V. Elanskaya ◽  
...  

Biochemistry ◽  
2003 ◽  
Vol 42 (9) ◽  
pp. 2748-2758 ◽  
Author(s):  
Sindra Peterson ◽  
Karin A. Åhrling ◽  
Joakim E. P. Högblom ◽  
Stenbjörn Styring

1984 ◽  
Vol 98 (1) ◽  
pp. 1-7 ◽  
Author(s):  
F A Wollman ◽  
P Delepelaire

We have used a new method to extensively modify the redox state of the plastoquinone pool in Chlamydomonas reinhardtii intact cells. This was achieved by an anaerobic treatment that inhibits the chlororespiratory pathway recently described by P. Bennoun (Proc. Natl. Acad. Sci. USA, 1982, 79:4352-4356). A state I (plus 3,4-dichlorophenyl-1,1-dimethylurea) leads to anaerobic state transition induced a decrease in the maximal fluorescence yield at room temperature and in the FPSII/FPSI ratio at 77 degrees K, which was three times larger than in a classical state I leads to state II transition. The fluorescence changes observed in vivo were similar in amplitude to those observed in vitro upon transfer to the light of dark-adapted, broken chloroplasts incubated in the presence of ATP. We then compared the phosphorylation pattern of thylakoid polypeptides in C. reinhardtii in vitro and in vivo using gamma-[32P]ATP and [32P]orthophosphate labeling, respectively. The same set of polypeptides, mainly light-harvesting complex polypeptides, was phosphorylated in both cases. We observed that this phosphorylation process is reversible and is mediated by the redox state of the plastoquinone pool in vivo as well as in vitro. Similar changes of even larger amplitude were observed with the F34 mutant intact cells lacking in photosystem II centers. The presence of the photosystem II centers is then not required for the occurrence of the plastoquinone-mediated phosphorylation of light-harvesting complex polypeptides.


Biochemistry ◽  
1995 ◽  
Vol 34 (48) ◽  
pp. 15721-15731 ◽  
Author(s):  
J. Kurreck ◽  
A. G. Seeliger ◽  
F. Reifarth ◽  
M. Karge ◽  
G. Renger

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