scholarly journals A unique regulation of the expression of the psbA, psbD, and psbE genes, encoding the D1, D2 and cytochrome b559 subunits of the Photosystem II complex in the chlorophyll d containing cyanobacterium Acaryochloris marina

2012 ◽  
Vol 1817 (7) ◽  
pp. 1083-1094 ◽  
Author(s):  
Éva Kiss ◽  
Péter B. Kós ◽  
Min Chen ◽  
Imre Vass
Keyword(s):  
Photosystem Ii ◽  
Cytochrome B559 ◽  
Genes Encoding ◽  
Acaryochloris Marina ◽  
Chlorophyll D

The nature of the photosystem II reaction centre in the chlorophyll d-containing prokaryote, Acaryochloris marina

2005 ◽  
Vol 4 (12) ◽  
pp. 1060 ◽  
Author(s):  
Min Chen ◽  
Alison Telfer ◽  
Su Lin ◽  
Andrew Pascal ◽  
Anthony W. D. Larkum ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Reaction Centre ◽  
Acaryochloris Marina ◽  
Chlorophyll D

scholarly journals Roles of Si and SiNPs in Improving Thermotolerance of Wheat Photosynthetic Machinery via Upregulation of PsbH, PsbB and PsbD Genes Encoding PSII Core Proteins

Horticulturae ◽  
2021 ◽  
Vol 7 (2) ◽  
pp. 16
Author(s):  
Heba Hassan ◽  
Aishah Alatawi ◽  
Awatif Abdulmajeed ◽  
Manal Emam ◽  
Hemmat Khattab
Keyword(s):  
Photosystem Ii ◽  
Global Climate ◽  
Soluble Sugars ◽  
Triticum Aestivum L ◽  
Pcr Analysis ◽  
Silicon Dioxide Nanoparticles ◽  
System Productivity ◽  
Photosynthetic System ◽  
Core Proteins ◽  
Genes Encoding

Photosystem II is extremely susceptible to environmental alterations, particularly high temperatures. The maintenance of an efficient photosynthetic system under stress conditions is one of the main issues for plants to attain their required energy. Nowadays, searching for stress alleviators is the main goal for maintaining photosynthetic system productivity and, thereby, crop yield under global climate change. Potassium silicate (K2SiO3, 1.5 mM) and silicon dioxide nanoparticles (SiO2NPs, 1.66 mM) were used to mitigate the negative impacts of heat stress (45 °C, 5 h) on wheat (Triticum aestivum L.) cv. (Shandawelly) seedlings. The results showed that K2SiO3 and SiO2NPs diminished leaf rolling symptoms and electrolyte leakage (EL) of heat-stressed wheat leaves. Furthermore, the maximum quantum yield of photosystem II (Fv/Fm) and the performance index (PIabs), as well as the photosynthetic pigments and organic solutes including soluble sugars, sucrose, and proline accumulation, were increased in K2SiO3 and SiO2NPs stressed leaves. At the molecular level, RT-PCR analysis showed that K2SiO3 and SiO2NPs treatments stimulated the overexpression of PsbH, PsbB, and PsbD genes. Notably, this investigation indicated that K2SiO3 was more effective in improving wheat thermotolerance compared to SiO2NPs. The application of K2SiO3 and SiO2NPs may be one of the proposed approaches to improve crop growth and productivity to tolerate climatic change.

Pigment exchange of Photosystem II reaction center by chlorophyll d

2005 ◽  
Vol 84 (1-3) ◽  
pp. 77-83 ◽  
Author(s):  
Tatsuya Tomo ◽  
Emi Hirano ◽  
Junko Nagata ◽  
Katsuyoshi Nakazato
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Chlorophyll D ◽  
Pigment Exchange

scholarly journals Mass spectrometry-based cross-linking study shows that the Psb28 protein binds to cytochrome b559 in Photosystem II

2017 ◽  
Vol 114 (9) ◽  
pp. 2224-2229 ◽  
Author(s):  
Daniel A. Weisz ◽  
Haijun Liu ◽  
Hao Zhang ◽  
Sundarapandian Thangapandian ◽  
Emad Tajkhorshid ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Photosystem Ii ◽  
Protein Interactions ◽  
Protein Complexes ◽  
Protein Docking ◽  
Cross Linking ◽  
Protein Protein Interactions ◽  
Cytochrome B559 ◽  
Reaction Center Complex ◽  
Assembly Intermediate

Photosystem II (PSII), a large pigment protein complex, undergoes rapid turnover under natural conditions. During assembly of PSII, oxidative damage to vulnerable assembly intermediate complexes must be prevented. Psb28, the only cytoplasmic extrinsic protein in PSII, protects the RC47 assembly intermediate of PSII and assists its efficient conversion into functional PSII. Its role is particularly important under stress conditions when PSII damage occurs frequently. Psb28 is not found, however, in any PSII crystal structure, and its structural location has remained unknown. In this study, we used chemical cross-linking combined with mass spectrometry to capture the transient interaction of Psb28 with PSII. We detected three cross-links between Psb28 and the α- and β-subunits of cytochrome b559, an essential component of the PSII reaction-center complex. These distance restraints enable us to position Psb28 on the cytosolic surface of PSII directly above cytochrome b559, in close proximity to the QB site. Protein–protein docking results also support Psb28 binding in this region. Determination of the Psb28 binding site and other biochemical evidence allow us to propose a mechanism by which Psb28 exerts its protective effect on the RC47 intermediate. This study also shows that isotope-encoded cross-linking with the “mass tags” selection criteria allows confident identification of more cross-linked peptides in PSII than has been previously reported. This approach thus holds promise to identify other transient protein–protein interactions in membrane protein complexes.

Identification of the Special Pair and ChlZ of Photosystem II in Acaryochloris marina

2008 ◽  
pp. 223-226
Author(s):  
Tatsuya Tomo ◽  
Tatsunori Okubo ◽  
Seiji Akimoto ◽  
Hideaki Miyashita ◽  
Tohru Tsuchiya ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Special Pair ◽  
Acaryochloris Marina
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