Light-Modulated Exposure of the Light-Harvesting Complex II (LHCII) to Protein Kinase(s) and State Transition inChlamydomonas reinhardtiiXanthophyll Mutants†

Biochemistry ◽  
2004 ◽  
Vol 43 (24) ◽  
pp. 7824-7833 ◽  
Author(s):  
Martin Vink ◽  
Hagit Zer ◽  
Noa Alumot ◽  
Ariel Gaathon ◽  
Krishna Niyogi ◽  
...  
1995 ◽  
Vol 50 (1-2) ◽  
pp. 77-85
Author(s):  
Manoj K. Joshi ◽  
Prasanna Mohanty ◽  
Salil Bose

Abstract Thylakoids isolated from SAN 9785 (4-chloro-5-dimethylamino-2-phenyl-3(2H)-pyridazi-none)-treated pea plants showed an inhibition of “state transition” and the light-harvesting complex II (LHC II) phosphorylation-mediated changes in the energy distribution between photosystem II (PS II) and photosystem I (PS I) as measured by a decrease in PS II and an increase in PS I fluorescence yield. Interestingly, in these thylakoids the extent of phosphorylation-induced migration of light-harvesting complex (LHC II-P) to non-appressed mem­brane regions was only marginally inhibited. We propose that the suppression in the ability for “state transition” by SANDOZ 9785 (SAN 9785) treatment occurs due to a lack of effec­tive coupling of the migrated LHC II-P and PS I. Since we observed a decrease in the antenna size of PS I of the treated plants, the lack of effective coupling is attributed to this decrease in the antenna size of PS I.


Biochemistry ◽  
2003 ◽  
Vol 42 (3) ◽  
pp. 728-738 ◽  
Author(s):  
Hagit Zer ◽  
Martin Vink ◽  
Susana Shochat ◽  
Reinhold G. Herrmann ◽  
Bertil Andersson ◽  
...  

2019 ◽  
Vol 476 (20) ◽  
pp. 2981-3018 ◽  
Author(s):  
Petar H. Lambrev ◽  
Parveen Akhtar

Abstract The light reactions of photosynthesis are hosted and regulated by the chloroplast thylakoid membrane (TM) — the central structural component of the photosynthetic apparatus of plants and algae. The two-dimensional and three-dimensional arrangement of the lipid–protein assemblies, aka macroorganisation, and its dynamic responses to the fluctuating physiological environment, aka flexibility, are the subject of this review. An emphasis is given on the information obtainable by spectroscopic approaches, especially circular dichroism (CD). We briefly summarise the current knowledge of the composition and three-dimensional architecture of the granal TMs in plants and the supramolecular organisation of Photosystem II and light-harvesting complex II therein. We next acquaint the non-specialist reader with the fundamentals of CD spectroscopy, recent advances such as anisotropic CD, and applications for studying the structure and macroorganisation of photosynthetic complexes and membranes. Special attention is given to the structural and functional flexibility of light-harvesting complex II in vitro as revealed by CD and fluorescence spectroscopy. We give an account of the dynamic changes in membrane macroorganisation associated with the light-adaptation of the photosynthetic apparatus and the regulation of the excitation energy flow by state transitions and non-photochemical quenching.


Author(s):  
Jianghao Wu ◽  
Liwei Rong ◽  
Weijun Lin ◽  
Lingxi Kong ◽  
Dengjie Wei ◽  
...  

Abstract In response to changing light quantity and quality, photosynthetic organisms perform state transitions, a process which optimizes photosynthetic yield and mitigates photo-damage. The serine/threonine-protein kinase STN7 phosphorylates the light-harvesting complex of photosystem II (PSII; light-harvesting complex II), which then migrates from PSII to photosystem I (PSI), thereby rebalancing the light excitation energy between the photosystems and restoring the redox poise of the photosynthetic electron transport chain. Two conserved cysteines forming intra- or intermolecular disulfide bonds in the lumenal domain (LD) of STN7 are essential for the kinase activity although it is still unknown how activation of the kinase is regulated. In this study, we show lumen thiol oxidoreductase 1 (LTO1) is co-expressed with STN7 in Arabidopsis (Arabidopsis thaliana) and interacts with the LD of STN7 in vitro and in vivo. LTO1 contains thioredoxin (TRX)-like and vitamin K epoxide reductase domains which are related to the disulfide-bond formation system in bacteria. We further show that the TRX-like domain of LTO1 is able to oxidize the conserved lumenal cysteines of STN7 in vitro. In addition, loss of LTO1 affects the kinase activity of STN7 in Arabidopsis. Based on these results, we propose that LTO1 helps to maintain STN7 in an oxidized active state in state 2 through redox interactions between the lumenal cysteines of STN7 and LTO1.


2004 ◽  
Vol 279 (35) ◽  
pp. 36884-36891 ◽  
Author(s):  
Joerg Standfuss ◽  
Werner Kühlbrandt

Sign in / Sign up

Export Citation Format

Share Document