The structure of PSI-LHCI from Cyanidium caldarium provides evolutionary insights into conservation and diversity of red-lineage LHCs

Author:

Kato Koji1ORCID,Hamaguchi Tasuku23,Kumazawa Minoru4ORCID,Nakajima Yoshiki1,Ifuku Kentaro4ORCID,Hirooka Shunsuke5ORCID,Hirose Yuu6ORCID,Miyagishima Shin-ya57ORCID,Suzuki Takehiro8,Kawakami Keisuke3ORCID,Dohmae Naoshi8ORCID,Yonekura Koji23ORCID,Shen Jian-Ren1ORCID,Nagao Ryo9ORCID

Affiliation:

1. Division of Photosynthesis and Structural Biology, Research Institute for Interdisciplinary Science, and Graduate School of Natural Science and Technology, Okayama University, Okayama 700-8530, Japan

2. Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Miyagi 980-8577, Japan

3. Biostructural Mechanism Laboratory, RIKEN SPring-8 Center, Hyogo 679-5148, Japan

4. Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan

5. Department of Gene Function and Phenomics, National Institute of Genetics, Shizuoka 411-8540, Japan

6. Department of Applied Chemistry and Life Science, Toyohashi University of Technology, Aichi 441-8580, Japan

7. Department of Genetics, The Graduate University for Advanced Studies (SOKENDAI), Shizuoka 411-8540, Japan

8. Biomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, Saitama 351-0198, Japan

9. Department of Applied Life Sciences, Faculty of Agriculture, Shizuoka University, Shizuoka 422-8529, Japan

Abstract

Light-harvesting complexes (LHCs) are diversified among photosynthetic organisms, and the structure of the photosystem I-LHC (PSI-LHCI) supercomplex has been shown to be variable depending on the species of organisms. However, the structural and evolutionary correlations of red-lineage LHCs are unknown. Here, we determined a 1.92-Å resolution cryoelectron microscopic structure of a PSI-LHCI supercomplex isolated from the red alga Cyanidium caldarium RK-1 (NIES-2137), which is an important taxon in the Cyanidiophyceae. We subsequently investigated the correlations of PSI-LHCIs from different organisms through structural comparisons and phylogenetic analysis. The PSI-LHCI structure obtained shows five LHCI subunits surrounding a PSI-monomer core. The five LHCIs are composed of two Lhcr1s, two Lhcr2s, and one Lhcr3. Phylogenetic analysis of LHCs bound to PSI in the red-lineage algae showed clear orthology of LHCs between C. caldarium and Cyanidioschyzon merolae , whereas no orthologous relationships were found between C. caldarium Lhcr1–3 and LHCs in other red-lineage PSI-LHCI structures. These findings provide evolutionary insights into conservation and diversity of red-lineage LHCs associated with PSI.

Funder

MEXT | Japan Society for the Promotion of Science

MEXT | JST | JST-Mirai Program

Publisher

Proceedings of the National Academy of Sciences

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