Structure of the red-shifted Fittonia albivenis photosystem I

Photosystem I (PSI) from Fittonia albivenis , an Acanthaceae ornamental plant, is notable among green plants for its red-shifted emission spectrum. Here, we solved the structure of a PSI–light harvesting complex I (LHCI) supercomplex from F. albivenis at 2.46-Å resolution using cryo-electron microsc...

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Published inNature communications Vol. 15; no. 1; pp. 6325 - 14
Main Authors Li, Xiuxiu, Huang, Guoqiang, Zhu, Lixia, Hao, Chenyang, Sui, Sen-Fang, Qin, Xiaochun
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 27.07.2024
Nature Publishing Group
Nature Portfolio
Subjects
101/28
631/449/1734/2075
631/449/1734/2077
631/45/535/1258
82/83
Acanthaceae
Amino Acid Sequence
Amino acids
Antennas
Binding sites
Chlorophyll
Chlorophyll - chemistry
Chlorophyll - metabolism
Chloroplasts
Cryoelectron Microscopy
Electron microscopy
Emission
Emissions
Energy
Energy harvesting
Humanities and Social Sciences
Life sciences
Light
Light-Harvesting Protein Complexes - chemistry
Light-Harvesting Protein Complexes - metabolism
Microscopy
Models, Molecular
multidisciplinary
Ornamental plants
Photochemistry
Photosynthesis
Photosystem I
Photosystem I Protein Complex - chemistry
Photosystem I Protein Complex - metabolism
Photosystem I Protein Complex - ultrastructure
Pigments
Plant Proteins - chemistry
Plant Proteins - metabolism
Prokaryotes
Proteins
Science
Science (multidisciplinary)
Structural members
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Abstract Photosystem I (PSI) from Fittonia albivenis , an Acanthaceae ornamental plant, is notable among green plants for its red-shifted emission spectrum. Here, we solved the structure of a PSI–light harvesting complex I (LHCI) supercomplex from F. albivenis at 2.46-Å resolution using cryo-electron microscopy. The supercomplex contains a core complex of 14 subunits and an LHCI belt with four antenna subunits (Lhca1–4) similar to previously reported angiosperm PSI–LHCI structures; however, Lhca3 differs in three regions surrounding a dimer of low-energy chlorophylls (Chls) termed red Chls, which absorb far-red beyond visible light. The unique amino acid sequences within these regions are exclusively shared by plants with strongly red-shifted fluorescence emission, suggesting candidate structural elements for regulating the energy state of red Chls. These results provide a structural basis for unraveling the mechanisms of light harvest and transfer in PSI–LHCI of under canopy plants and for designing Lhc to harness longer-wavelength light in the far-red spectral range. Fittonia albivenis is shade-adapted ornamental plant that can efficiently use far-red light for photosynthesis. Here the authors describe the structure of the red-shifted F. albivenis photosystem I to give insights into how plants can use far-red light to drive photochemistry.
AbstractList Abstract Photosystem I (PSI) from Fittonia albivenis, an Acanthaceae ornamental plant, is notable among green plants for its red-shifted emission spectrum. Here, we solved the structure of a PSI–light harvesting complex I (LHCI) supercomplex from F. albivenis at 2.46-Å resolution using cryo-electron microscopy. The supercomplex contains a core complex of 14 subunits and an LHCI belt with four antenna subunits (Lhca1–4) similar to previously reported angiosperm PSI–LHCI structures; however, Lhca3 differs in three regions surrounding a dimer of low-energy chlorophylls (Chls) termed red Chls, which absorb far-red beyond visible light. The unique amino acid sequences within these regions are exclusively shared by plants with strongly red-shifted fluorescence emission, suggesting candidate structural elements for regulating the energy state of red Chls. These results provide a structural basis for unraveling the mechanisms of light harvest and transfer in PSI–LHCI of under canopy plants and for designing Lhc to harness longer-wavelength light in the far-red spectral range.
Photosystem I (PSI) from Fittonia albivenis, an Acanthaceae ornamental plant, is notable among green plants for its red-shifted emission spectrum. Here, we solved the structure of a PSI-light harvesting complex I (LHCI) supercomplex from F. albivenis at 2.46-Å resolution using cryo-electron microscopy. The supercomplex contains a core complex of 14 subunits and an LHCI belt with four antenna subunits (Lhca1-4) similar to previously reported angiosperm PSI-LHCI structures; however, Lhca3 differs in three regions surrounding a dimer of low-energy chlorophylls (Chls) termed red Chls, which absorb far-red beyond visible light. The unique amino acid sequences within these regions are exclusively shared by plants with strongly red-shifted fluorescence emission, suggesting candidate structural elements for regulating the energy state of red Chls. These results provide a structural basis for unraveling the mechanisms of light harvest and transfer in PSI-LHCI of under canopy plants and for designing Lhc to harness longer-wavelength light in the far-red spectral range.Photosystem I (PSI) from Fittonia albivenis, an Acanthaceae ornamental plant, is notable among green plants for its red-shifted emission spectrum. Here, we solved the structure of a PSI-light harvesting complex I (LHCI) supercomplex from F. albivenis at 2.46-Å resolution using cryo-electron microscopy. The supercomplex contains a core complex of 14 subunits and an LHCI belt with four antenna subunits (Lhca1-4) similar to previously reported angiosperm PSI-LHCI structures; however, Lhca3 differs in three regions surrounding a dimer of low-energy chlorophylls (Chls) termed red Chls, which absorb far-red beyond visible light. The unique amino acid sequences within these regions are exclusively shared by plants with strongly red-shifted fluorescence emission, suggesting candidate structural elements for regulating the energy state of red Chls. These results provide a structural basis for unraveling the mechanisms of light harvest and transfer in PSI-LHCI of under canopy plants and for designing Lhc to harness longer-wavelength light in the far-red spectral range.
Photosystem I (PSI) from Fittonia albivenis, an Acanthaceae ornamental plant, is notable among green plants for its red-shifted emission spectrum. Here, we solved the structure of a PSI-light harvesting complex I (LHCI) supercomplex from F. albivenis at 2.46-Å resolution using cryo-electron microscopy. The supercomplex contains a core complex of 14 subunits and an LHCI belt with four antenna subunits (Lhca1-4) similar to previously reported angiosperm PSI-LHCI structures; however, Lhca3 differs in three regions surrounding a dimer of low-energy chlorophylls (Chls) termed red Chls, which absorb far-red beyond visible light. The unique amino acid sequences within these regions are exclusively shared by plants with strongly red-shifted fluorescence emission, suggesting candidate structural elements for regulating the energy state of red Chls. These results provide a structural basis for unraveling the mechanisms of light harvest and transfer in PSI-LHCI of under canopy plants and for designing Lhc to harness longer-wavelength light in the far-red spectral range.
Photosystem I (PSI) from Fittonia albivenis , an Acanthaceae ornamental plant, is notable among green plants for its red-shifted emission spectrum. Here, we solved the structure of a PSI–light harvesting complex I (LHCI) supercomplex from F. albivenis at 2.46-Å resolution using cryo-electron microscopy. The supercomplex contains a core complex of 14 subunits and an LHCI belt with four antenna subunits (Lhca1–4) similar to previously reported angiosperm PSI–LHCI structures; however, Lhca3 differs in three regions surrounding a dimer of low-energy chlorophylls (Chls) termed red Chls, which absorb far-red beyond visible light. The unique amino acid sequences within these regions are exclusively shared by plants with strongly red-shifted fluorescence emission, suggesting candidate structural elements for regulating the energy state of red Chls. These results provide a structural basis for unraveling the mechanisms of light harvest and transfer in PSI–LHCI of under canopy plants and for designing Lhc to harness longer-wavelength light in the far-red spectral range. Fittonia albivenis is shade-adapted ornamental plant that can efficiently use far-red light for photosynthesis. Here the authors describe the structure of the red-shifted F. albivenis photosystem I to give insights into how plants can use far-red light to drive photochemistry.
Photosystem I (PSI) from Fittonia albivenis, an Acanthaceae ornamental plant, is notable among green plants for its red-shifted emission spectrum. Here, we solved the structure of a PSI–light harvesting complex I (LHCI) supercomplex from F. albivenis at 2.46-Å resolution using cryo-electron microscopy. The supercomplex contains a core complex of 14 subunits and an LHCI belt with four antenna subunits (Lhca1–4) similar to previously reported angiosperm PSI–LHCI structures; however, Lhca3 differs in three regions surrounding a dimer of low-energy chlorophylls (Chls) termed red Chls, which absorb far-red beyond visible light. The unique amino acid sequences within these regions are exclusively shared by plants with strongly red-shifted fluorescence emission, suggesting candidate structural elements for regulating the energy state of red Chls. These results provide a structural basis for unraveling the mechanisms of light harvest and transfer in PSI–LHCI of under canopy plants and for designing Lhc to harness longer-wavelength light in the far-red spectral range.Fittonia albivenis is shade-adapted ornamental plant that can efficiently use far-red light for photosynthesis. Here the authors describe the structure of the red-shifted F. albivenis photosystem I to give insights into how plants can use far-red light to drive photochemistry.
ArticleNumber 6325
Author Li, Xiuxiu
Huang, Guoqiang
Sui, Sen-Fang
Qin, Xiaochun
Zhu, Lixia
Hao, Chenyang
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  surname: Qin
  fullname: Qin, Xiaochun
  email: bio_qinxc@ujn.edu.cn
  organization: School of Chemistry and Chemical Engineering, School of Biological Science and Technology, University of Jinan
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SSID ssj0000391844
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Snippet Photosystem I (PSI) from Fittonia albivenis , an Acanthaceae ornamental plant, is notable among green plants for its red-shifted emission spectrum. Here, we...
Photosystem I (PSI) from Fittonia albivenis, an Acanthaceae ornamental plant, is notable among green plants for its red-shifted emission spectrum. Here, we...
Abstract Photosystem I (PSI) from Fittonia albivenis, an Acanthaceae ornamental plant, is notable among green plants for its red-shifted emission spectrum....
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proquest
pubmed
crossref
springer
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Publisher
StartPage 6325
SubjectTerms 101/28
631/449/1734/2075
631/449/1734/2077
631/45/535/1258
82/83
Acanthaceae
Amino Acid Sequence
Amino acids
Antennas
Binding sites
Chlorophyll
Chlorophyll - chemistry
Chlorophyll - metabolism
Chloroplasts
Cryoelectron Microscopy
Electron microscopy
Emission
Emissions
Energy
Energy harvesting
Humanities and Social Sciences
Life sciences
Light
Light-Harvesting Protein Complexes - chemistry
Light-Harvesting Protein Complexes - metabolism
Microscopy
Models, Molecular
multidisciplinary
Ornamental plants
Photochemistry
Photosynthesis
Photosystem I
Photosystem I Protein Complex - chemistry
Photosystem I Protein Complex - metabolism
Photosystem I Protein Complex - ultrastructure
Pigments
Plant Proteins - chemistry
Plant Proteins - metabolism
Prokaryotes
Proteins
Science
Science (multidisciplinary)
Structural members
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Title Structure of the red-shifted Fittonia albivenis photosystem I
URI https://link.springer.com/article/10.1038/s41467-024-50655-9
https://www.ncbi.nlm.nih.gov/pubmed/39060282
https://www.proquest.com/docview/3085026355
https://www.proquest.com/docview/3085116433
https://doaj.org/article/51873d3195ca44deb81262f7af43b1c7
Volume 15
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