scholarly journals Thermal Stress, Aggregation of Chlorophyll-Protein Complexes, and Light-Dependent Recovery of PSII activity in Wheat Seedlings

2021 ◽  
Vol 68 (5) ◽  
pp. 867-872
Author(s):  
M. S. Khristin ◽  
T. N. Smolova ◽  
V. D. Kreslavski
Keyword(s):  
Low Temperature ◽  
Structural Changes ◽  
Protein Complexes ◽  
Red Light ◽  
Photochemical Activity ◽  
Wheat Seedlings ◽  
Psii Activity ◽  
Temperature Spectra ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein

Abstract The dynamics of changes in the photochemical activity of photosystem II (PSII) and low-temperature spectra at 77 K in the first leaves of 11-day winter wheat plants Triticum aestivum L., as well as structural changes in chlorophyll-protein complexes (CPC) of thylakoid membranes during recovery after a short-term (20 min) heating at a temperature of 42°C, were studied. Changes in the Fv/Fm, F735/F695, and F735/F685 ratios indicate inhibition of PSII immediately after heating. Using nondenaturing electrophoresis, it was shown that the light-harvesting Chl a/b complex of PSII does not aggregate immediately after heating but after several hours, after 6 h the desagregation of CPC was observed, which was consistent with an increase in the Fv/Fm ratio upon recovery. The influence of temperature, intensity, and quality of light (white, blue, and red light) on the recovery of PSII activity and low-temperature fluorescence spectra was studied. It was concluded that the recovery is a photo-activated low-energy process, independent of photosynthesis, and the most effective in blue light.

scholarly journals ИССЛЕДОВАНИЕ ФОТОХИМИЧЕСКИХ СВОЙСТВ И ФИЛОГЕНИИ РАСТИТЕЛЬНЫХ БЕЛКОВ СЕМЕЙСТВА WSCP

2020 ◽  
Vol 3 (11(80)) ◽  
pp. 38-43
Author(s):  
Yu. Obuhov ◽  
K. Neverov ◽  
Yu. Maleeva ◽  
M. Krickij
Keyword(s):  
Search Algorithm ◽  
Protein Complexes ◽  
Red Light ◽  
Bioinformatic Analysis ◽  
Class Ii ◽  
Photochemical Activity ◽  
Water Soluble ◽  
Pigment Protein Complexes ◽  
Chlorophyll Protein Complexes ◽  
The Difference

Here we show the ability of the chlorophyll associated with proteins of the WSCP family (Water-Soluble Chlorophyll-binding Proteins) to photosensitize oxidative redox reactions. Irradiation with red light of the recombinant chlorophyll-protein complexes WSCP subclasses IIa and IIb in the presence of an electron donor (NADH) led to oxidation of the donor, i.e., these pigment-protein complexes showed photochemical activity. Meanwhile there was no photodestruction of chlorophyll associated with WSCP, which indicates the photocatalytic nature of the detected redox reaction. The kinetic constants of NADH photooxidation were higher for WSCP subclass IIa (BoWSCP) than for subclass IIb (LvWSCP). To explain the difference in the photosensitizing activity of representatives of different WSCP subclasses, bioinformatic analysis of class II proteins of this family was carried out. For this purpose, we searched for members of the WSCP family in the UniProt protein sequence database using the BLAST search algorithm, followed by their multiple alignment and construction of a phylogenetic tree using the EMBL-EBI Clustal Omega web service and the MEGA7 program. Bioinformatic analysis has confirmed the phylogenetic division of the WSCP class II protein family into two subclasses, previously established on the basis of the difference in their physicochemical properties. It was suggested that phylogeny is related to the photochemical activity of representatives of different subclasses in the WSCP family.

scholarly journals Structural changes and lateral redistribution of photosystem II during donor side photoinhibition of thylakoids.

1992 ◽  
Vol 119 (2) ◽  
pp. 325-335 ◽  
Author(s):  
R Barbato ◽  
G Friso ◽  
F Rigoni ◽  
F Dalla Vecchia ◽  
G M Giacometti
Keyword(s):  
Photosystem Ii ◽  
Photosystem I ◽  
Structural Changes ◽  
Protein Complexes ◽  
Gradient Centrifugation ◽  
Photosynthetic Apparatus ◽  
Topological Stability ◽  
Donor Side ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein

The structural and topological stability of thylakoid components under photoinhibitory conditions (4,500 microE.m-2.s-1 white light) was studied on Mn depleted thylakoids isolated from spinach leaves. After various exposures to photoinhibitory light, the chlorophyll-protein complexes of both photosystems I and II were separated by sucrose gradient centrifugation and analysed by Western blotting, using a set of polyclonals raised against various apoproteins of the photosynthetic apparatus. A series of events occurring during donor side photoinhibition are described for photosystem II, including: (a) lowering of the oligomerization state of the photosystem II core; (b) cleavage of 32-kD protein D1 at specific sites; (c) dissociation of chlorophyll-protein CP43 from the photosystem II core; and (d) migration of damaged photosystem II components from the grana to the stroma lamellae. A tentative scheme for the succession of these events is illustrated. Some effects of photoinhibition on photosystem I are also reported involving dissociation of antenna chlorophyll-proteins LHCI from the photosystem I reaction center.

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