Uphill energy transfer mechanism for photosynthesis in an Antarctic alga.

Autor: Kosugi M; Astrobiology Center, 2-21-1 Osawa, Mitaka, Tokyo, 181-8588, Japan. mkosugi@nibb.ac.jp.; National Astronomical Observatory of Japan, 2-21-1 Osawa, Mitaka, Tokyo, 181-8588, Japan. mkosugi@nibb.ac.jp.; Department of Biological Sciences, Faculty of Science and Engineering, Chuo University, 1-13-27 Kasuga, Bunkyo-ku, Tokyo, 112-8551, Japan. mkosugi@nibb.ac.jp.; National Institute for Basic Biology, National Institutes of Natural Science, 38 Nishigonaka, Myodaiji, Okazaki, Aichi, 444-8585, Japan. mkosugi@nibb.ac.jp., Kawasaki M; Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), 1-1 Oho, Tsukuba, Ibaraki, 305-0801, Japan.; Department of Materials Structure Science, School of High Energy Accelerator Science, The Graduate University of Advanced Studies (Soken-dai), 1-1 Oho, Tsukuba, Ibaraki, 305-0801, Japan., Shibata Y; Department of Chemistry, Graduate School of Science, Tohoku University, 6-3 Aza Aoba Aramaki, Aoba-ku, Sendai, 980-8578, Japan. shibata@m.tohoku.ac.jp., Hara K; Department of Biological Production, Akita Prefectural University, 241-438 Kaidobata-nishi, Shimoshinjo-nakano, Akita, 010-0195, Japan., Takaichi S; Department of Molecular Microbiology, Tokyo University of Agriculture, 1-1 Sakuragaoka, Setagaya-ku, Tokyo, 156-8502, Japan., Moriya T; Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), 1-1 Oho, Tsukuba, Ibaraki, 305-0801, Japan., Adachi N; Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), 1-1 Oho, Tsukuba, Ibaraki, 305-0801, Japan., Kamei Y; National Institute for Basic Biology, National Institutes of Natural Sciences, 38 Nishigonaka, Myodaiji, Okazaki, Aichi, 444-8585, Japan.; Department of Basic Biology, School of Life Sciences, SOKENDAI (The Graduate University for Advanced Studies), 38 Nishigonaka, Myodaiji, Okazaki, Aichi, 444-8585, Japan., Kashino Y; Graduate School of Science, University of Hyogo, 3-2-1 Kohto, Kamigohri, Ako-gun, Hyogo, 678-1297, Japan., Kudoh S; National Institute of Polar Research, Research Organization of Information and Systems, 10-3 Midori-cho, Tachikawa, Tokyo, 190-8518, Japan.; Department of Polar Science, School of Multidisciplinary Science, SOKENDAI (The Graduate University for Advanced Studies), 10-3 Midori-cho, Tachikawa, Tokyo, 190-8518, Japan., Koike H; Department of Biological Sciences, Faculty of Science and Engineering, Chuo University, 1-13-27 Kasuga, Bunkyo-ku, Tokyo, 112-8551, Japan., Senda T; Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), 1-1 Oho, Tsukuba, Ibaraki, 305-0801, Japan. toshiya.senda@kek.jp.; Department of Materials Structure Science, School of High Energy Accelerator Science, The Graduate University of Advanced Studies (Soken-dai), 1-1 Oho, Tsukuba, Ibaraki, 305-0801, Japan. toshiya.senda@kek.jp.; Faculty of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-8572, Japan. toshiya.senda@kek.jp.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2023 Feb 15; Vol. 14 (1), pp. 730. Date of Electronic Publication: 2023 Feb 15.
DOI: 10.1038/s41467-023-36245-1
Abstrakt: 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.
(© 2023. The Author(s).)
Databáze: MEDLINE
Externí odkaz: