Retraction Note: Light Harvesting-like Protein 3 Interacts with Phytoene Synthase and Is Necessary for Carotenoid and Chlorophyll Biosynthesis in Rice

Abstract Background Carotenoid biosynthesis is essential for the generation of photosynthetic pigments, phytohormone production, and flower color development. The light harvesting like 3 (LIL3) protein, which belongs to the light-harvesting complex protein family in photosystems, interacts with geranylgeranyl reductase (GGR) and protochlorophyllide oxidoreductase (POR) both of which are known to regulate terpenoid and chlorophyll biosynthesis, respectively, in both rice and Arabidopsis. Results In our study, a CRISPR-Cas9 generated 4-bp deletion mutant oslil3 showed aberrant chloroplast development, growth defects, low fertility rates and reduced pigment contents. A comparative transcriptomic analysis of oslil3 suggested that differentially expressed genes (DEGs) involved in photosynthesis, cell wall modification, primary and secondary metabolism are differentially regulated in the mutant. Protein-protein interaction assays indicated that LIL3 interacts with phytoene synthase (PSY) and in addition the gene expression of PSY genes are regulated by LIL3. Subcellular localization of LIL3 and PSY suggested that both are thylakoid membrane anchored proteins in the chloroplast. We suggest that LIL3 directly interacts with PSY to regulate carotenoid biosynthesis. Conclusion This study reveals a new role of LIL3 in regulating pigment biosynthesis through interaction with the rate limiting enzyme PSY in carotenoid biosynthesis in rice presenting it as a putative target for genetic manipulation of pigment biosynthesis pathways in crop plants.

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Green Bacteria: Chlorophyll Biosynthesis, Light-Harvesting, Reaction Centers, and Electron Transport

Encyclopedia of Biological Chemistry ◽

10.1016/b978-0-12-378630-2.00159-6 ◽

2013 ◽

pp. 501-509

Author(s):

D.A. Bryant

Keyword(s):

Electron Transport ◽

Light Harvesting ◽

Chlorophyll Biosynthesis ◽

Reaction Centers ◽

Green Bacteria

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Functional and mutational analysis of the light-harvesting chlorophyll a/b protein of thylakoid membranes.

The Journal of Cell Biology ◽

10.1083/jcb.102.3.972 ◽

1986 ◽

Vol 102 (3) ◽

pp. 972-981 ◽

Cited By ~ 111

Author(s):

B D Kohorn ◽

E Harel ◽

P R Chitnis ◽

J P Thornber ◽

E M Tobin

Keyword(s):

Chlorophyll A ◽

Thylakoid Membrane ◽

Mutational Analysis ◽

Light Harvesting ◽

Chlorophyll Biosynthesis ◽

Thylakoid Membranes ◽

Stable Complex ◽

Coding Region ◽

Light Harvesting Complexes ◽

Lhc Ii

The precursor for a Lemna light-harvesting chlorophyll a/b protein (pLHCP) has been synthesized in vitro from a single member of the nuclear LHCP multigene family. We report the sequence of this gene. When incubated with Lemna chloroplasts, the pLHCP is imported and processed into several polypeptides, and the mature form is assembled into the light-harvesting complex of photosystem II (LHC II). The accumulation of the processed LHCP is enhanced by the addition to the chloroplasts of a precursor and a co-factor for chlorophyll biosynthesis. Using a model for the arrangement of the mature polypeptide in the thylakoid membrane as a guide, we have created mutations that lie within the mature coding region. We have studied the processing, the integration into thylakoid membranes, and the assembly into light-harvesting complexes of six of these deletions. Four different mutant LHCPs are found as processed proteins in the thylakoid membrane, but only one appears to have an orientation in the membrane that is similar to that of the wild type. No mutant LHCP appears in LHC II. The other two mutant LHCPs cannot be detected within the chloroplasts. We conclude that stable complex formation is not required for the processing and insertion of altered LHCPs into the thylakoid membrane. We discuss the results in light of our model.

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High-Resolution electron crystallography of the light-harvesting chlorophyll-a/b protein complex from chloroplast membranes

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100181816 ◽

1990 ◽

Vol 48 (1) ◽

pp. 610-610

Author(s):

Werner Kühlbrandt ◽

Da Neng Wang ◽

K.H. Downing

Keyword(s):

High Resolution ◽

Electron Diffraction ◽

Chlorophyll A ◽

Protein Complex ◽

Structural Integrity ◽

Light Harvesting ◽

Lhc Ii ◽

Diffraction Patterns ◽

Difference Fourier ◽

2D Crystals

The light-harvesting chlorophyll-a/b protein complex (LHC-II) is the most abundant membrane protein in the chloroplasts of green plants where it functions as a molecular antenna of solar energy for photosynthesis. We have grown two-dimensional (2d) crystals of the purified, detergent-solubilized LHC-II . The crystals which measured 5 to 10 μm in diameter were stabilized for electron microscopy by washing with a 0.5% solution of tannin. Electron diffraction patterns of untilted 2d crystals cooled to 130 K showed sharp spots to 3.1 Å resolution. Spot-scan images of 2d crystals were recorded at 160 K with the Berkeley microscope . Images of untilted crystals were processed, using the unbending procedure by Henderson et al . A projection map of the complex at 3.7Å resolution was generated from electron diffraction amplitudes and high-resolution phases obtained by image processing .A difference Fourier analysis with the same image phases and electron diffraction amplitudes recorded of frozen, hydrated specimens showed no significant differences in the 3.7Å projection map. Our tannin treatment therefore does not affect the structural integrity of the complex.

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Macroorganisation and flexibility of thylakoid membranes

Biochemical Journal ◽

10.1042/bcj20190080 ◽

2019 ◽

Vol 476 (20) ◽

pp. 2981-3018 ◽

Cited By ~ 8

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.

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