Uphill energy transfer mechanism for photosynthesis in an Antarctic alga
© 2023. The Author(s)..
Prasiola crispa, an aerial green alga, forms layered colonies under the severe terrestrial conditions of Antarctica. Since only far-red light is available at a deep layer of the colony, P. crispa has evolved a molecular system for photosystem II (PSII) excitation using far-red light with uphill energy transfer. However, the molecular basis underlying this system remains elusive. Here, we purified a light-harvesting chlorophyll (Chl)-binding protein complex from P. crispa (Pc-frLHC) that excites PSII with far-red light and revealed its ring-shaped structure with undecameric 11-fold symmetry at 3.13 Å resolution. The primary structure suggests that Pc-frLHC evolved from LHCI rather than LHCII. The circular arrangement of the Pc-frLHC subunits is unique among eukaryote LHCs and forms unprecedented Chl pentamers at every subunit‒subunit interface near the excitation energy exit sites. The Chl pentamers probably contribute to far-red light absorption. Pc-frLHC's unique Chl arrangement likely promotes PSII excitation with entropy-driven uphill excitation energy transfer.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2023 |
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| Erschienen: |
2023 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:14 |
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| Enthalten in: |
Nature communications - 14(2023), 1 vom: 15. Feb., Seite 730 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Kosugi, Makiko [VerfasserIn] |
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| Links: |
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| Themen: |
1406-65-1 |
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| Anmerkungen: |
Date Completed 17.02.2023 Date Revised 09.03.2023 published: Electronic Citation Status MEDLINE |
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| doi: |
10.1038/s41467-023-36245-1 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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NLM352994398 |
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| 520 | |a Prasiola crispa, an aerial green alga, forms layered colonies under the severe terrestrial conditions of Antarctica. Since only far-red light is available at a deep layer of the colony, P. crispa has evolved a molecular system for photosystem II (PSII) excitation using far-red light with uphill energy transfer. However, the molecular basis underlying this system remains elusive. Here, we purified a light-harvesting chlorophyll (Chl)-binding protein complex from P. crispa (Pc-frLHC) that excites PSII with far-red light and revealed its ring-shaped structure with undecameric 11-fold symmetry at 3.13 Å resolution. The primary structure suggests that Pc-frLHC evolved from LHCI rather than LHCII. The circular arrangement of the Pc-frLHC subunits is unique among eukaryote LHCs and forms unprecedented Chl pentamers at every subunit‒subunit interface near the excitation energy exit sites. The Chl pentamers probably contribute to far-red light absorption. Pc-frLHC's unique Chl arrangement likely promotes PSII excitation with entropy-driven uphill excitation energy transfer | ||
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| 700 | 1 | |a Kawasaki, Masato |e verfasserin |4 aut | |
| 700 | 1 | |a Shibata, Yutaka |e verfasserin |4 aut | |
| 700 | 1 | |a Hara, Kojiro |e verfasserin |4 aut | |
| 700 | 1 | |a Takaichi, Shinichi |e verfasserin |4 aut | |
| 700 | 1 | |a Moriya, Toshio |e verfasserin |4 aut | |
| 700 | 1 | |a Adachi, Naruhiko |e verfasserin |4 aut | |
| 700 | 1 | |a Kamei, Yasuhiro |e verfasserin |4 aut | |
| 700 | 1 | |a Kashino, Yasuhiro |e verfasserin |4 aut | |
| 700 | 1 | |a Kudoh, Sakae |e verfasserin |4 aut | |
| 700 | 1 | |a Koike, Hiroyuki |e verfasserin |4 aut | |
| 700 | 1 | |a Senda, Toshiya |e verfasserin |4 aut | |
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