Cryo-EM structural analyses of chlorophyll b-enriched PSI-LHC and PSII-LHC supercomplexes of the siphonous green alga Bryopsis corticulans.
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| Formato: | Artículo científico |
| Lenguaje: | en |
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Plant communications
2026
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| _version_ | 1868266095179202560 |
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| author | Liu, Xueyang Li, Zhenhua Shen, Liangliang Shen, Lili Wu, Bin Li, Xiaoyi Yang, Yanyan Gao, Shan Han, Guangye Kuang, Tingyun Liu, Cheng Shen, Jian-Ren Wang, Wenda |
| author_facet | Liu, Xueyang Li, Zhenhua Shen, Liangliang Shen, Lili Wu, Bin Li, Xiaoyi Yang, Yanyan Gao, Shan Han, Guangye Kuang, Tingyun Liu, Cheng Shen, Jian-Ren Wang, Wenda Liu, Xueyang Li, Zhenhua Shen, Liangliang Shen, Lili Wu, Bin Li, Xiaoyi Yang, Yanyan Gao, Shan Han, Guangye Kuang, Tingyun Liu, Cheng Shen, Jian-Ren Wang, Wenda |
| collection | PubMed - marine biology |
| contents | Cryo-EM structural analyses of chlorophyll b-enriched PSI-LHC and PSII-LHC supercomplexes of the siphonous green alga Bryopsis corticulans. Liu, Xueyang Li, Zhenhua Shen, Liangliang Shen, Lili Wu, Bin Li, Xiaoyi Yang, Yanyan Gao, Shan Han, Guangye Kuang, Tingyun Liu, Cheng Shen, Jian-Ren Wang, Wenda Cryoelectron Microscopy Light-Harvesting Protein Complexes Chlorophyll Photosystem II Protein Complex Photosystem I Protein Complex Chlorophyta The light-harvesting complexes of photosystem I (PSI) and PSII (LHCI and LHCII) in Bryopsis corticulans (B. corticulans) are homologous to those in Chlamydomonas reinhardtii and land plants but exhibit a distinct chlorophyll (Chl) and carotenoid composition. Here, we report cryo-electron microscopy structures of the PSI-LHCI-LHCII supercomplex, comprising three LHCII trimers, and the CSMN-type PSII-LHCII supercomplex from B. corticulans. In the PSI supercomplex, ten LHCI subunits assemble into two belts and one heterodimer, coordinating a total of 86 Chl a and 65 Chl b molecules (Chl a/b ratio of 1.3, compared with 3.4 in C. reinhardtii), as well as 18 siphonaxanthin, 2 siphonein, and 13 α-carotene molecules. Of the three LHCII trimers bound to the PSI-LHCI supercomplex, two are anchored to the PSI core primarily via phosphorylated subunits, whereas the third, non-phosphorylated trimer is stabilized through interactions with Lhca-d and the adjacent LHCII trimer. In the CSMN-type PSII-LHCII supercomplex, the N-LHCII is positioned closer to the PSII core than in C. reinhardtii, likely owing to loss of the linker motif in the N-terminal region of B. corticulans CP29. Structure-based energy transfer analysis suggests that this spatial rearrangement enhances the efficiency of excitation energy transfer from N-LHCII to the PSII core. Collectively, these findings reveal structural adaptations that underlie the acclimation strategies of siphonous green algae inhabiting intertidal environments. |
| format | Artículo científico |
| id | pubmed_41578646 |
| institution | PubMed |
| language | en |
| publishDate | 2026 |
| publisher | Plant communications |
| record_format | pubmed |
| spellingShingle | Cryo-EM structural analyses of chlorophyll b-enriched PSI-LHC and PSII-LHC supercomplexes of the siphonous green alga Bryopsis corticulans. Liu, Xueyang Li, Zhenhua Shen, Liangliang Shen, Lili Wu, Bin Li, Xiaoyi Yang, Yanyan Gao, Shan Han, Guangye Kuang, Tingyun Liu, Cheng Shen, Jian-Ren Wang, Wenda Cryoelectron Microscopy Light-Harvesting Protein Complexes Chlorophyll Photosystem II Protein Complex Photosystem I Protein Complex Chlorophyta Cryo-EM structural analyses of chlorophyll b-enriched PSI-LHC and PSII-LHC supercomplexes of the siphonous green alga Bryopsis corticulans. Liu, Xueyang Li, Zhenhua Shen, Liangliang Shen, Lili Wu, Bin Li, Xiaoyi Yang, Yanyan Gao, Shan Han, Guangye Kuang, Tingyun Liu, Cheng Shen, Jian-Ren Wang, Wenda Cryoelectron Microscopy Light-Harvesting Protein Complexes Chlorophyll Photosystem II Protein Complex Photosystem I Protein Complex Chlorophyta The light-harvesting complexes of photosystem I (PSI) and PSII (LHCI and LHCII) in Bryopsis corticulans (B. corticulans) are homologous to those in Chlamydomonas reinhardtii and land plants but exhibit a distinct chlorophyll (Chl) and carotenoid composition. Here, we report cryo-electron microscopy structures of the PSI-LHCI-LHCII supercomplex, comprising three LHCII trimers, and the CSMN-type PSII-LHCII supercomplex from B. corticulans. In the PSI supercomplex, ten LHCI subunits assemble into two belts and one heterodimer, coordinating a total of 86 Chl a and 65 Chl b molecules (Chl a/b ratio of 1.3, compared with 3.4 in C. reinhardtii), as well as 18 siphonaxanthin, 2 siphonein, and 13 α-carotene molecules. Of the three LHCII trimers bound to the PSI-LHCI supercomplex, two are anchored to the PSI core primarily via phosphorylated subunits, whereas the third, non-phosphorylated trimer is stabilized through interactions with Lhca-d and the adjacent LHCII trimer. In the CSMN-type PSII-LHCII supercomplex, the N-LHCII is positioned closer to the PSII core than in C. reinhardtii, likely owing to loss of the linker motif in the N-terminal region of B. corticulans CP29. Structure-based energy transfer analysis suggests that this spatial rearrangement enhances the efficiency of excitation energy transfer from N-LHCII to the PSII core. Collectively, these findings reveal structural adaptations that underlie the acclimation strategies of siphonous green algae inhabiting intertidal environments. |
| title | Cryo-EM structural analyses of chlorophyll b-enriched PSI-LHC and PSII-LHC supercomplexes of the siphonous green alga Bryopsis corticulans. |
| topic | Cryoelectron Microscopy Light-Harvesting Protein Complexes Chlorophyll Photosystem II Protein Complex Photosystem I Protein Complex Chlorophyta |
| url | https://pubmed.ncbi.nlm.nih.gov/41578646/ |