Asymmetric structure of the native Rhodobacter sphaeroides dimeric LH1–RC complex

Kazutoshi Tani (), Ryo Kanno, Riku Kikuchi, Saki Kawamura, Kenji V. P. Nagashima, Malgorzata Hall, Ai Takahashi, Long-Jiang Yu, Yukihiro Kimura, Michael T. Madigan, Akira Mizoguchi, Bruno M. Humbel and Zheng-Yu Wang-Otomo ()
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Kazutoshi Tani: Mie University
Ryo Kanno: Okinawa Institute of Science and Technology Graduate University (OIST), 1919-1, Tancha, Onna-son, Kunigami-gun
Riku Kikuchi: Ibaraki University
Saki Kawamura: Ibaraki University
Kenji V. P. Nagashima: Kanagawa University, 2946 Tsuchiya
Malgorzata Hall: Okinawa Institute of Science and Technology Graduate University (OIST), 1919-1, Tancha, Onna-son, Kunigami-gun
Ai Takahashi: Okinawa Institute of Science and Technology Graduate University (OIST), 1919-1, Tancha, Onna-son, Kunigami-gun
Long-Jiang Yu: Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences
Yukihiro Kimura: Kobe University
Michael T. Madigan: Southern Illinois University
Akira Mizoguchi: Mie University
Bruno M. Humbel: Okinawa Institute of Science and Technology Graduate University (OIST), 1919-1, Tancha, Onna-son, Kunigami-gun
Zheng-Yu Wang-Otomo: Ibaraki University

Nature Communications, 2022, vol. 13, issue 1, 1-9

Abstract: Abstract 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 (ΔU). 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 β-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 ΔU LH1–RC monomer was half-moon-shaped and contained 11 α- and 10 β-polypeptides, indicating a critical role for protein-U in controlling the number of αβ-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.

Date: 2022
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DOI: 10.1038/s41467-022-29453-8

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