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Uphill energy transfer mechanism for photosynthesis in an Antarctic alga

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 ener...

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Detalles Bibliográficos
Autores principales: Kosugi, Makiko, Kawasaki, Masato, Shibata, Yutaka, Hara, Kojiro, Takaichi, Shinichi, Moriya, Toshio, Adachi, Naruhiko, Kamei, Yasuhiro, Kashino, Yasuhiro, Kudoh, Sakae, Koike, Hiroyuki, Senda, Toshiya
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9931709/
https://www.ncbi.nlm.nih.gov/pubmed/36792917
http://dx.doi.org/10.1038/s41467-023-36245-1
Descripción
Sumario: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.