Gene Regulation of Chlorophyll Biosynthesis

A special issue of Plants (ISSN 2223-7747). This special issue belongs to the section "Plant Genetics, Genomics and Biotechnology".

Deadline for manuscript submissions: closed (31 January 2022) | Viewed by 5912

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Laboratory of Plant Molecular Genetics and Laboratory of Environmental and Systems Biology, Grenoble‐Alpes‐University Grenoble, 38400 Saint-Martin-d'Hères, France
Interests: plant developmental biology; chloroplast biogenesis; tetrapyrroles; plant hormone action; abiotic stress responses
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Dear Colleagues,

Chlorophyll is a plant-specific tetrapyrrole that performs major roles in the light trapping and energy transduction processes during photosynthesis. It is synthesized from glutamate via a complex metabolic shunt comprising 16 reactions taking place in the chloroplast. Much progress has been made to define these steps and characterize the genes and enzymes controlling chlorophyll biosynthesis. Key regulatory steps of chlorophyll biosynthesis in higher plants involve 5-aminolevulinic acid formation, the production of Mg2+-protoporphyrin IX, and the light-dependent reduction of protochlorophyllide (Pchlide). Light-dependent and light-independent Pchlide reductases haven been identified in nature, and their characterization has provided important insights into the evolution of chlorophyll biosynthesis. Because both linear and cyclic tetrapyrroles are highly reactive and can trigger the formation of reactive oxygen species (ROS), the biosynthesis of chlorophyll must be tightly regulated in time and space such that no damage occurs to cellular and subcellular structures. It is the aim of this Special Issue to summarize our current knowledge of the genes and enzymes involved in chlorophyll biosynthesis and what strategies living organisms have evolved to cope with the undesired, potentially harmful effects of these tetrapyrrole compounds.

Prof. Dr. Steffen Reinbothe
Guest Editor

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Keywords

  • Tetrapyrrole synthesis 
  • Chloroplast development 
  • C5-pathway enzymes 
  • Enzyme structure and function 
  • Gene regulation

Published Papers (2 papers)

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Research

13 pages, 2363 KiB  
Article
Effects of Light and Oxygen on Chlorophyll d Biosynthesis in a Marine Cyanobacterium Acaryochloris marina
by Yuki Tsuzuki, Yusuke Tsukatani, Hisanori Yamakawa, Shigeru Itoh, Yuichi Fujita and Haruki Yamamoto
Plants 2022, 11(7), 915; https://doi.org/10.3390/plants11070915 - 29 Mar 2022
Cited by 5 | Viewed by 2825
Abstract
A marine cyanobacterium Acaryochloris marina synthesizes chlorophyll (Chl) d as a major Chl. Chl d has a formyl group at its C3 position instead of a vinyl group in Chl a. This modification allows Chl d to absorb far-red light addition to [...] Read more.
A marine cyanobacterium Acaryochloris marina synthesizes chlorophyll (Chl) d as a major Chl. Chl d has a formyl group at its C3 position instead of a vinyl group in Chl a. This modification allows Chl d to absorb far-red light addition to visible light, yet the enzyme catalyzing the formation of the C3-formyl group has not been identified. In this study, we focused on light and oxygen, the most important external factors in Chl biosynthesis, to investigate their effects on Chl d biosynthesis in A. marina. The amount of Chl d in heterotrophic dark-grown cells was comparable to that in light-grown cells, indicating that A. marina has a light-independent pathway for Chl d biosynthesis. Under anoxic conditions, the amount of Chl d increased with growth in light conditions; however, no growth was observed in dark conditions, indicating that A. marina synthesizes Chl d normally even under such “micro-oxic” conditions caused by endogenous oxygen production. Although the oxygen requirement for Chl d biosynthesis could not be confirmed, interestingly, accumulation of pheophorbide d was observed in anoxic and dark conditions, suggesting that Chl d degradation is induced by anaerobicity and darkness. Full article
(This article belongs to the Special Issue Gene Regulation of Chlorophyll Biosynthesis)
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15 pages, 3712 KiB  
Article
Extracellular Vesicle-Mediated Secretion of Protochlorophyllide in the Cyanobacterium Leptolyngbya boryana
by Kentaro Usui, Haruki Yamamoto, Takao Oi, Mitsutaka Taniguchi, Hitoshi Mori and Yuichi Fujita
Plants 2022, 11(7), 910; https://doi.org/10.3390/plants11070910 - 29 Mar 2022
Cited by 2 | Viewed by 2336
Abstract
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Gene Regulation of Chlorophyll Biosynthesis)
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