Your browser doesn't support javascript.
loading
Structures and organizations of PSI-AcpPCI supercomplexes from red tidal and coral symbiotic photosynthetic dinoflagellates.
Li, Xiaoyi; Li, Zhenhua; Wang, Fangfang; Zhao, Songhao; Xu, Caizhe; Mao, Zhiyuan; Duan, Jialin; Feng, Yue; Yang, Yang; Shen, Lili; Wang, Guanglei; Yang, Yanyan; Yu, Long-Jiang; Sang, Min; Han, Guangye; Wang, Xuchu; Kuang, Tingyun; Shen, Jian-Ren; Wang, Wenda.
Afiliação
  • Li X; Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
  • Li Z; Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
  • Wang F; College of Life Sciences, University of Chinese Academy of Science, Beijing 100049, China.
  • Zhao S; National Facility for Protein Science in Shanghai, Chinese Academy of Sciences, Shanghai 201204, China.
  • Xu C; Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
  • Mao Z; College of Life Sciences, University of Chinese Academy of Science, Beijing 100049, China.
  • Duan J; Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
  • Feng Y; Department of Mechanical Engineering, Tsinghua University, Beijing 100084, China.
  • Yang Y; Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
  • Shen L; College of Life Sciences, University of Chinese Academy of Science, Beijing 100049, China.
  • Wang G; National Facility for Protein Science in Shanghai, Chinese Academy of Sciences, Shanghai 201204, China.
  • Yang Y; Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
  • Yu LJ; College of Life Sciences, University of Chinese Academy of Science, Beijing 100049, China.
  • Sang M; Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
  • Han G; Laboratory for Ecology of Tropical Islands, Ministry of Education, College of Life Sciences, Hainan Normal University, Haikou 571158, China.
  • Wang X; Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
  • Kuang T; College of Life Sciences, University of Chinese Academy of Science, Beijing 100049, China.
  • Shen JR; Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
  • Wang W; College of Life Sciences, University of Chinese Academy of Science, Beijing 100049, China.
Proc Natl Acad Sci U S A ; 121(7): e2315476121, 2024 Feb 13.
Article em En | MEDLINE | ID: mdl-38319970
ABSTRACT
Marine photosynthetic dinoflagellates are a group of successful phytoplankton that can form red tides in the ocean and also symbiosis with corals. These features are closely related to the photosynthetic properties of dinoflagellates. We report here three structures of photosystem I (PSI)-chlorophylls (Chls) a/c-peridinin protein complex (PSI-AcpPCI) from two species of dinoflagellates by single-particle cryoelectron microscopy. The crucial PsaA/B subunits of a red tidal dinoflagellate Amphidinium carterae are remarkably smaller and hence losing over 20 pigment-binding sites, whereas its PsaD/F/I/J/L/M/R subunits are larger and coordinate some additional pigment sites compared to other eukaryotic photosynthetic organisms, which may compensate for the smaller PsaA/B subunits. Similar modifications are observed in a coral symbiotic dinoflagellate Symbiodinium species, where two additional core proteins and fewer AcpPCIs are identified in the PSI-AcpPCI supercomplex. The antenna proteins AcpPCIs in dinoflagellates developed some loops and pigment sites as a result to accommodate the changed PSI core, therefore the structures of PSI-AcpPCI supercomplex of dinoflagellates reveal an unusual protein assembly pattern. A huge pigment network comprising Chls a and c and various carotenoids is revealed from the structural analysis, which provides the basis for our deeper understanding of the energy transfer and dissipation within the PSI-AcpPCI supercomplex, as well as the evolution of photosynthetic organisms.
Assuntos
Palavras-chave

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Dinoflagellida / Antozoários Limite: Animals Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2024 Tipo de documento: Article País de afiliação: China

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Dinoflagellida / Antozoários Limite: Animals Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2024 Tipo de documento: Article País de afiliação: China