Chlorophyll-binding subunits of photosystem I and II: Biosynthesis, chlorophyll incorporation and assembly

Komenda, Josef; Sobotka, Roman

doi:10.1016/bs.abr.2019.02.001

Cited by 19 publications

(20 citation statements)

References 131 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As an essential cofactor of photosystem I and II, chlorophylls play a fundamental role in photosynthesis, since they are responsible for both the absorption of visible light and its photochemical conversion within the cell [27]. Chlorophyll a is in a higher concentration than chlorophyll b, commonly 3:1 [28], so chlorophyll a is more susceptible to being affected by environmental factors as CNMs.…”

Section: Discussionmentioning

confidence: 99%

Impact of Carbon Nanomaterials on the Antioxidant System of Tomato Seedlings

González‐García

López-Vargas

Cadenas‐Pliego³

et al. 2019

IJMS

View full text Add to dashboard Cite

Tomato is one of the most economically important vegetables worldwide and is constantly threatened by various biotic and abiotic stress factors reducing the quality and quantity in the production of this crop. As an alternative to mitigate stress in plants, carbon nanomaterials (CNMs) have been used in agricultural areas. Therefore, the objective of the present work was to evaluate the antioxidant responses of tomato seedlings to the application via foliar and drench of carbon nanotubes (CNTs) and graphene (GP). Different doses (10, 50, 100, 250, 500, and 1000 mg L−1) and a control were evaluated. The results showed that the fresh and dry root weight increased with the application of CNMs. Regarding the antioxidant responses of tomato seedlings, the application of CNMs increased the content of phenols, flavonoids, ascorbic acid, glutathione, photosynthetic pigments, activity of the enzyme’s ascorbate peroxidase, glutathione peroxidase, catalase, and phenylalanine ammonia lyase as well as the content of proteins. Therefore, the use of carbon-based nanomaterials could be a good alternative to induce tolerance to different stress in tomato crop.

show abstract

Section: Discussionmentioning

confidence: 99%

Impact of Carbon Nanomaterials on the Antioxidant System of Tomato Seedlings

González‐García

López-Vargas

Cadenas‐Pliego³

et al. 2019

IJMS

View full text Add to dashboard Cite

show abstract

“…Chlorophyll (Chl) is a tetrapyrrole pigment essential for photosynthesis. In cyanobacteria, Chl a is biosynthesized via 15 sequential enzymatic reactions that begin with glutamate [ 1 , 2 ], and the resulting Chl molecules eventually bind to Chl-binding proteins, such as PsaA/B proteins [ 3 , 4 , 5 , 6 ]. Protochlorophyllide (Pchlide) reduction, the penultimate reaction, in Chl a biosynthesis, is catalyzed by two enzymes with different evolutionary origins: light-dependent Pchlide reductase (LPOR) [ 7 , 8 ] and dark-operative Pchlide reductase (DPOR) [ 9 , 10 ] ( Figure 1 ).…”

Section: Introductionmentioning

confidence: 99%

Extracellular Vesicle-Mediated Secretion of Protochlorophyllide in the Cyanobacterium Leptolyngbya boryana

Usui

Yamamoto

et al. 2022

Plants

View full text Add to dashboard Cite

Protochlorophyllide (Pchlide) reduction in the late stage of chlorophyll a (Chl) biosynthesis is catalyzed by two enzymes: light-dependent Pchlide oxidoreductase (LPOR) and dark-operative Pchlide oxidoreductase (DPOR). The differential operation of LPOR and DPOR enables a stable supply of Chl in response to changes in light conditions and environmental oxygen levels. When a DPOR-deficient mutant (YFC2) of the cyanobacterium Leptolyngbya boryana is grown heterotrophically in the dark, Pchlide accumulates in the cells and is secreted into the culture medium. In this study, we demonstrated the extracellular vesicle-mediated secretion of Pchlide. Pchlide fractions were isolated from the culture medium using sucrose density gradient centrifugation. Mass spectrometry analysis revealed that the Pchlide fractions contained porin isoforms, TolC, and FG-GAP repeat-containing protein, which are localized in the outer membrane. Transmission electron microscopy revealed extracellular vesicle-like structures in the vicinity of YFC2 cells and the Pchlide fractions. These findings suggested that the Pchlide secretion is mediated by extracellular vesicles in dark-grown YFC2 cells.

show abstract

“…The PSII core contains approximately fifteen proteins in 1:1 stoichiometry, which serve as scaffolds to organize the numerous pigments and prosthetic groups that mediate light-absorption, charge separation and electron transport. This structure is assembled in an ordered pathway with the assistance of accessory factors that are, in many cases, conserved between cyanobacteria and chloroplasts [3]. Furthermore, PSII is a highly dynamic structure due to the damaging effects of light on its D1 reaction center protein.…”

Section: Introductionmentioning

confidence: 99%

“…We focus on mutants lacking four nucleus-encoded proteins: OHP1, OHP2, HCF244, and HCF136. These proteins are conserved in cyanobacteria, where the OHP orthologs are named HliD and HliC, the HCF244 ortholog is named Ycf39, and the HCF136 ortholog is named Ycf48 (reviewed in [3]). Recent work has provided evidence that OHP1, OHP2, and HCF244 (and their cyanobacterial counterparts) comprise a complex required for the addition of nascent D1 to a D2/PsbE/PsbF-containing assembly intermediate [13][14][15][16][17].…”

Section: Introductionmentioning

confidence: 99%

Exploring the Link between Photosystem II Assembly and Translation of the Chloroplast psbA mRNA

Chotewutmontri

Williams‐Carrier

Barkan

2020

Plants

View full text Add to dashboard Cite

Photosystem II (PSII) in chloroplasts and cyanobacteria contains approximately fifteen core proteins, which organize numerous pigments and prosthetic groups that mediate the light-driven water-splitting activity that drives oxygenic photosynthesis. The PSII reaction center protein D1 is subject to photodamage, whose repair requires degradation of damaged D1 and its replacement with nascent D1. Mechanisms that couple D1 synthesis with PSII assembly and repair are poorly understood. We address this question by using ribosome profiling to analyze the translation of chloroplast mRNAs in maize and Arabidopsis mutants with defects in PSII assembly. We found that OHP1, OHP2, and HCF244, which comprise a recently elucidated complex involved in PSII assembly and repair, are each required for the recruitment of ribosomes to psbA mRNA, which encodes D1. By contrast, HCF136, which acts upstream of the OHP1/OHP2/HCF244 complex during PSII assembly, does not have this effect. The fact that the OHP1/OHP2/HCF244 complex brings D1 into proximity with three proteins with dual roles in PSII assembly and psbA ribosome recruitment suggests that this complex is the hub of a translational autoregulatory mechanism that coordinates D1 synthesis with need for nascent D1 during PSII biogenesis and repair.

show abstract

Chlorophyll-binding subunits of photosystem I and II: Biosynthesis, chlorophyll incorporation and assembly

Cited by 19 publications

References 131 publications

Impact of Carbon Nanomaterials on the Antioxidant System of Tomato Seedlings

Impact of Carbon Nanomaterials on the Antioxidant System of Tomato Seedlings

Extracellular Vesicle-Mediated Secretion of Protochlorophyllide in the Cyanobacterium Leptolyngbya boryana

Exploring the Link between Photosystem II Assembly and Translation of the Chloroplast psbA mRNA

Contact Info

Product

Resources

About