Seasonal variations of leaf chlorophyll–protein complexes in the wintergreen herbaceous plant Ajuga reptans L.

2018 ◽  
Vol 45 (5) ◽  
pp. 519 ◽  
Author(s):  
Olga Dymova ◽  
Mikhail Khristin ◽  
Zbigniew Miszalski ◽  
Andrzej Kornas ◽  
Kazimierz Strzalka ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Carotenoid Content ◽  
Protective Mechanism ◽  
Herbaceous Plant ◽  
Light Harvesting Complex ◽  
Chl A ◽  
Ajuga Reptans ◽  
Light Harvesting Complex Ii ◽  
Different Seasons ◽  
Chlorophyll Protein Complexes

The chlorophyll and carotenoid content, and the spectra of low-temperature fluorescence of the leaves, chloroplasts and isolated pigment–protein complexes in the perennial herbaceous wintergreen plant Ajuga reptans L. (bugle) in different seasons of the year were studied. During winter, these plants downregulate photosynthesis and the PSA is reorganised, including the loss of chlorophyll, possible reductions in the number of functional reaction centres of PSII, and changes in aggregation of the thylakoid protein complexes. We also observed a restructuring of the PSI–PSII megacomplex and the PSII–light-harvesting complex II supercomplex in leaves covered by snow. After snowmelt, the monomeric form of the chl a/b pigment–protein complex associated with PSII (LHCII) and the free pigments were also detected. We expect that snow cover provides favourable conditions for keeping photosynthetic machinery ready for photosynthesis in spring just after snowmelt. During winter, the role of the zeaxanthin-dependent protective mechanism, which is responsible for the dissipation of excess absorbed light energy, is likely to increase.

scholarly journals Role of the HSP70 Homologue from Chloroplasts in the Assembly of the Photosynthetic Apparatus

1993 ◽  
Author(s):  
Rachel Nechushtai ◽  
Parag Chitnis
Keyword(s):  
Protein Complexes ◽  
Photosynthetic Apparatus ◽  
Crop Productivity ◽  
Cdna Clones ◽  
Light Harvesting Complex ◽  
Complex Protein ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein

The major goal of the proposed research was to study the role of a 70-kDa heat shock cognate protein from chloroplasts (ct-HSP70) in the assembly of chlorophyll-protein complexes. The latters are mostly important in allowing photosynthesis to occur. Photosynthesis is at the heart of crop productivity and the knowledge of the biogenesis of the photosynthetic apparatus is essential to manipulate the efficiency of photosynthesis. The characterization of the function of the ct-HSP70 was planned to be studied in vitro by assaying its capability to physically interact with the thylakoid proteins and to assist their assembly into thylakoid membranes. We planned to identify regions in the light-harvesting complex protein (LHCP) that interact with the ct-HSP70 and characterize the interaction between them. We also intended to isolate cDNA clones encoding ct-HSP70, sequence them, express one of them in E. coli and use the purified protein for functional assays. The research in this BARD proposal aimed at providing insights and aid in understanding the mechanism by which plants may respond to the heat stress. Since plants often experience increased temperatures.

scholarly journals Temperature-mediated shifts in chlorophyll biosynthesis in leaves of chlorophyll b-lacking rice (Oryza sativa L.)

2021 ◽  
Vol 49 (2) ◽  
pp. 12306
Author(s):  
Khiem Minh NGUYEN ◽  
Zhi-Wei YANG ◽  
Tin-Han SHIH ◽  
Szu-Hsien LIN ◽  
Jun-Wei LIN ◽  
...  
Keyword(s):  
Crop Yields ◽  
Oryza Sativa L ◽  
Chlorophyll Biosynthesis ◽  
Differentially Expressed Gene ◽  
Growth And Yield ◽  
Light Harvesting Complex ◽  
Chl A ◽  
Light Harvesting Complex Ii ◽  
Influence Of Temperature On ◽  
Chl Biosynthesis

Extreme temperatures have become a threat to crop yields. To maintain plant growth and yield, chlorophyll (Chl) biosynthesis plays a crucial role in adaptation to temperature stress. This study investigated the influence of temperature on the biosynthesis and characteristics of pigments (Chl a, Chl b, and carotenoids) in the leaves of Chl b-lacking mutant rice (Chlorina 1, ch1) and wild-type rice (Norin No.8, wt). The ch1 showed thinner stacked grana caused by a decrease in thylakoid membranes per granum at 15 °C, whereas the destacked grana were observed at 35 °C after 12 h incubation. However, the grana are stacked normally, along with the absence of Chl b, and a significantly decreased amount of Chl a in both wt and ch1 were observed after heat stress exposure, demonstrating that light-harvesting complex II proteins are involved in grana stacking. Ch1 was sensitive to 15 °C during the first 4 h of incubation but it subsequently adapted to the cold environment. In addition, there were no significant differences in the photosynthesis between wt and ch1 after 12 h incubation at 35 °C. Differentially expressed gene (DEGs) analysis revealed that GluRS expression decreased, which resulted in a decline in Chl biosynthesis in wt and ch1 at 35 °C. At 8 h and 12 h, there were no significant differences in the expression of DEGs involved in Chl biosynthesis and degradation between wt and ch1 at 15 °C. ALAD expression in wt and ch1 at 15 °C decreased until it was undetectable. These findings suggested that ch1 may adapt to temperatures ranging from 15 °C to 35 °C.

Significance of protein crowding, order and mobility for photosynthetic membrane functions

2008 ◽  
Vol 36 (5) ◽  
pp. 967-970 ◽  
Author(s):  
Helmut Kirchhoff
Keyword(s):  
Large Scale ◽  
Protein Complexes ◽  
Photosynthetic Apparatus ◽  
Lateral Diffusion ◽  
Functional Communication ◽  
Protein Diffusion ◽  
Higher Plant ◽  
Photosynthetic Membrane ◽  
Light Harvesting Complex ◽  
Light Harvesting Complex Ii

Natural photosynthesis requires diffusion-based processes either for the functional communication of protein complexes or for the adaptation, maintenance and biogenesis of the photosynthetic apparatus. A conceptual problem with lateral diffusion in photosynthetic membranes arises from the fact that these membranes are densely packed with membrane integral protein complexes (molecular crowding). Theoretical analysis of PQ (plastoquinone) and protein diffusion in higher plant grana thylakoids reveal very inefficient lateral diffusion. In contrast, measurement of protein mobility in grana membranes shows that a fraction of protein complexes can move surprisingly fast. It is postulated that organization of protein complexes in supercomplexes and large-scale ordering of Photosystem II and light-harvesting complex II could be strategies for the optimization of diffusion in crowded thylakoid membranes.

Growth and development at cold-hardening temperatures. Chlorophyll–protein complexes and thylakoid membrane polypeptides

1984 ◽  
Vol 62 (1) ◽  
pp. 61-67 ◽  
Author(s):  
B. Elfman ◽  
N. P. A. Huner ◽  
M. Griffith ◽  
M. Krol ◽  
W. G. Hopkins ◽  
...  
Keyword(s):  
Growth And Development ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Thylakoid Membranes ◽  
Cold Hardening ◽  
Complex Iv ◽  
Light Harvesting Complex ◽  
Dodecyl Sulfate ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein

Chlorophyll–protein complexes of thylakoid membranes from rye plants (Secale cereale L. cv. Puma) grown at warm and cold-hardening temperatures were investigated by gel electrophoresis. Complex IV from cold-grown tissue was detectable in the presence of dodecyl sulfate if and only if solubilization and electrophoresis were performed at 4 °C, whereas complex IV from warm-grown material was detectable if membrane solubilization and electrophoresis were performed at either 4 or 23 °C in the presence of dodecyl sulfate. In the presence of octyl-β-D-glucopyranoside, the chlorophyll–protein complexes from cold-grown tissue were less stable at 23 °C than those from warm-grown tissue. Regardless of the detergent used, there was always more oligomer of the light-harvesting complex present in samples prepared from thylakoid membranes of warm-grown tissue than those from membranes of cold-grown tissue. It is concluded that the pigment–protein interaction in those complexes associated with photosystem II and the light-harvesting chlorophyll a/b – protein complex has been altered upon growth and development at cold-hardening temperatures.

scholarly journals The orf162b Sequence ofRhodobacter capsulatus Encodes a Protein Required for Optimal Levels of Photosynthetic Pigment-Protein Complexes

2000 ◽  
Vol 182 (19) ◽  
pp. 5440-5447 ◽  
Author(s):  
Muktak Aklujkar ◽  
Andrea L. Harmer ◽  
Roger C. Prince ◽  
J. Thomas Beatty
Keyword(s):  
Rhodobacter Capsulatus ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Photosynthetic Pigment ◽  
Photosynthetic Apparatus ◽  
Coding Region ◽  
Reading Frame ◽  
Light Harvesting Complex ◽  
Pseudostationary Phase ◽  
Light Harvesting Complex Ii

ABSTRACT The orf162b sequence, the second open reading frame 3′ of the reaction center (RC) H protein gene puhA in theRhodobacter capsulatus photosynthesis gene cluster, is shown to be transcribed from a promoter located 5′ of puhA. A nonpolar mutation of orf162b was generated by replacing most of the coding region with an antibiotic resistance cartridge. Although the mutant strain initiated rapid photosynthetic growth, growth slowed progressively and cultures often entered a pseudostationary phase. The amounts of the RC and light harvesting complex I (LHI) in cells obtained from such photosynthetic cultures were abnormally low, but these deficiencies were less severe when the mutant was grown to a pseudostationary phase induced by low aeration in the absence of illumination. The orf162b mutation did not significantly affect the expression of apufB::lacZ translationally in-frame gene fusion under the control of the puf promoter, indicating normal transcription and translation of RC and LHI genes. Spontaneous secondary mutations in the strain with theorf162b disruption resulted in a bypass of the photosynthetic growth retardation and reduced the level of light harvesting complex II. These results and the presence of sequences similar to orf162b in other species indicate that the Orf162b protein is required for normal levels of the photosynthetic apparatus in purple photosynthetic bacteria.

Photosynthesis, Pigment–Protein Complexes and Electronic Energy Transport: Simple Models for Complicated Processes

2017 ◽  
Vol 100 (3) ◽  
pp. 313-330
Author(s):  
Lewis A. Baker ◽  
Scott Habershon
Keyword(s):  
Energy Transport ◽  
Environmental Changes ◽  
Protein Complexes ◽  
Electronic Energy ◽  
Quantum Dynamic ◽  
Transport Networks ◽  
Light Harvesting Complex ◽  
Light Harvesting Complex Ii ◽  
Pigment Protein Complexes ◽  
Qualitative Picture

In this review, we discuss our recent work on modelling biological pigment–protein complexes, such as the Fenna–Matthews–Olson complex and light-harvesting complex-II, to explain their electronic energy transport properties. In particular, we highlight how a network-based analysis approach, where the light-absorbing pigments are treated as a network of interconnected nodes, can provide a qualitative picture of quantum dynamic energy transport. With this in mind, we demonstrate how other properties such as robustness to environmental changes can be assessed in a simple and computationally tractable manner. Such analyses could prove useful for the design of artificial energy transport networks such as those which might find application in solar cells.

Macroorganisation and flexibility of thylakoid membranes

2019 ◽  
Vol 476 (20) ◽  
pp. 2981-3018 ◽  
Author(s):  
Petar H. Lambrev ◽  
Parveen Akhtar
Keyword(s):  
Light Harvesting ◽  
Current Knowledge ◽  
Three Dimensional ◽  
Photosynthetic Apparatus ◽  
Dynamic Responses ◽  
State Transitions ◽  
Photochemical Quenching ◽  
Light Harvesting Complex ◽  
Complex Ii ◽  
Light Harvesting Complex Ii

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.

Photoinhibition in vivo and in vitro Involves Weakly Coupled Chlorophyll–Protein Complexes‡¶

2002 ◽  
Vol 75 (6) ◽  
pp. 613 ◽  
Author(s):  
Stefano Santabarbara ◽  
Ilaria Cazzalini ◽  
Andrea Rivadossi ◽  
Flavio M. Garlaschi ◽  
Giuseppe Zucchelli ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Weakly Coupled ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein

scholarly journals Transcriptome and proteome analysis suggest enhanced photosynthesis in tetraploid Liriodendron sino-americanum

2021 ◽  
Author(s):  
Tingting Chen ◽  
Yu Sheng ◽  
Zhaodong Hao ◽  
Xiaofei Long ◽  
Fangfang Fu ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Protein Complexes ◽  
Proteome Analysis ◽  
Tree Height ◽  
Photosynthetic Electron Transport ◽  
Industrial Applications ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein ◽  
Photosynthesis Genes ◽  
Underlying Mechanisms

Abstract Polyploidy generally provides an advantage in phenotypic variation and growth vigor. However, the underlying mechanisms remain poorly understood. The tetraploid L. sino-americanum exhibits altered morphology compared to its diploid counterpart, including larger, thicker and deeper green leaves, bigger stomata, thicker stems and increased tree height. Such characteristics can be useful in ornamental and industrial applications. To elucidate the molecular mechanisms behind this variation, we performed a comparative transcriptome and proteome analysis. Our transcriptome data indicated that some photosynthesis genes and pathways were differentially altered and enriched in tetraploid L. sino-americanum, mainly related to F-type ATPase, the cytochrome b6/f complex, photosynthetic electron transport, the light harvesting chlorophyll protein complexes, photosystem I and II. Most of the differentially expressed proteins we could identify are also involved in photosynthesis. Our physiological results showed that tetraploids have an enhanced photosynthetic capacity, concomitant with great levels of sugar and starch in leaves. This suggests that tetraploid L. sino-americanum might experience comprehensive transcriptome reprogramming of genes related to photosynthesis. This study has especially emphasized molecular changes involved in photosynthesis that accompany polyploidy, and provides a possible explanation for the altered phenotype of polyploidy plants in comparison to their diploid form.

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