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Asymmetric structure of the native Rhodobacter sphaeroides dimeric LH1-RC complex
Tani, Kazutoshi; Kanno, Ryo; Kikuchi, Riku; Kawamura, Saki; Nagashima, Kenji V. P.; Hall, Malgorzata; Takahashi, Ai; Yu, Long-Jiang; Kimura, Yukihiro5; Madigan, Michael T.; Mizoguchi, Akira; Humbel, Bruno M.; Wang-Otomo, Zheng-Yu
2022
发表期刊NATURE COMMUNICATIONS
卷号13期号:1
摘要Rhodobacter sphaeroides is a model organism for studying bacterial photosynthesis. Here, the authors present structures of its native dimeric and a protein-U-lacking monomeric light-harvesting-reaction center complexes, which reveal asymmetric features for the dimer and an altered shape for the monomer. Rhodobacter sphaeroides is a model organism in bacterial photosynthesis, and its light-harvesting-reaction center (LH1-RC) complex contains both dimeric and monomeric forms. Here we present cryo-EM structures of the native LH1-RC dimer and an LH1-RC monomer lacking protein-U (Delta U). The native dimer reveals several asymmetric features including the arrangement of its two monomeric components, the structural integrity of protein-U, the overall organization of LH1, and rigidities of the proteins and pigments. PufX plays a critical role in connecting the two monomers in a dimer, with one PufX interacting at its N-terminus with another PufX and an LH1 beta-polypeptide in the other monomer. One protein-U was only partially resolved in the dimeric structure, signaling different degrees of disorder in the two monomers. The Delta U LH1-RC monomer was half-moon-shaped and contained 11 alpha- and 10 beta-polypeptides, indicating a critical role for protein-U in controlling the number of alpha beta-subunits required for dimer assembly and stabilization. These features are discussed in relation to membrane topology and an assembly model proposed for the native dimeric complex.
学科领域Multidisciplinary Sciences
DOI10.1038/s41467-022-29453-8
收录类别SCI
语种英语
WOS关键词PHOTOSYNTHETIC CORE COMPLEX ; RC-LH1-PUFX COMPLEX ; PUFX ; DIMERIZATION ; PROTEIN ; ORGANIZATION ; ARCHITECTURE ; MEMBRANES ; SUBUNIT
WOS研究方向Science Citation Index Expanded (SCI-EXPANDED)
WOS记录号WOS:000779784400002
出版者NATURE PORTFOLIO
文献子类Article
出版地BERLIN
EISSN2041-1723
资助机构Platform Project for Supporting Drug Discovery and Life Science Research (Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)) from AMED [JP20am0101118, 1758, JP20am0101116, 1878, 17am0101116j0001, 18am0101116j0002, 19am0101116j0003] ; Okinawa Institute of Science and Technology ; Japanese Cabinet Office ; National Key R&D Program of China [2019YFA0904600] ; JSPS KAKENHI [JP16H04174, JP18H05153, JP20H05086, JP20H02856]
作者邮箱ktani@doc.medic.mie-u.ac.jp ; wang@ml.ibaraki.ac.jp
作品OA属性Green Submitted, Green Published, gold
引用统计
被引频次:14[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ibcas.ac.cn/handle/2S10CLM1/28760
专题中科院光生物学重点实验室
作者单位1.Mie Univ, Grad Sch Med, Tsu, Mie 5148507, Japan
2.Kanno, Ryo; Hall, Malgorzata; Takahashi, Ai; Humbel, Bruno M.] Okinawa Inst Sci & Technol Grad Univ OIST, Res Support Div, Imaging Sect, 1919-1 Tancha, Onna, Okinawa 9040495, Japan
3.Ibaraki Univ, Fac Sci, Mito, Ibaraki 3108512, Japan
4.Nagashima, Kenji V. P.] Kanagawa Univ, Res Inst Integrated Sci, 2946 Tsuchiya, Hiratsuka, Kanagawa 2591293, Japan
5.Chinese Acad Sci, Inst Bot, Key Lab Photobiol, Photosynth Res Ctr, Beijing 100093, Peoples R China
6.Kobe Univ, Grad Sch Agr, Dept Agrobiosci, Nada Ku, Kobe, Hyogo 6578501, Japan
7.Madigan, Michael T.] Southern Illinois Univ, Sch Biol Sci, Dept Microbiol, Carbondale, IL 62901 USA
推荐引用方式
GB/T 7714
Tani, Kazutoshi,Kanno, Ryo,Kikuchi, Riku,et al. Asymmetric structure of the native Rhodobacter sphaeroides dimeric LH1-RC complex[J]. NATURE COMMUNICATIONS,2022,13(1).
APA Tani, Kazutoshi.,Kanno, Ryo.,Kikuchi, Riku.,Kawamura, Saki.,Nagashima, Kenji V. P..,...&Wang-Otomo, Zheng-Yu.(2022).Asymmetric structure of the native Rhodobacter sphaeroides dimeric LH1-RC complex.NATURE COMMUNICATIONS,13(1).
MLA Tani, Kazutoshi,et al."Asymmetric structure of the native Rhodobacter sphaeroides dimeric LH1-RC complex".NATURE COMMUNICATIONS 13.1(2022).
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