Structural basis for the absence of low-energy chlorophylls in a photosystem I trimer from Gloeobacter violaceus
Photosystem I (PSI) is a multi-subunit pigment-protein complex that functions in light-harvesting and photochemical charge-separation reactions, followed by reduction of NADP to NADPH required for CO2 fixation in photosynthetic organisms. PSI from different photosynthetic organisms has a variety of...
| Main Authors: | , , , , , , , , , , , , , |
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| Format: | Article |
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eLife Sciences Publications Ltd
2022-04-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/73990 |
| _version_ | 1811236665187893248 |
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| author | Koji Kato Tasuku Hamaguchi Ryo Nagao Keisuke Kawakami Yoshifumi Ueno Takehiro Suzuki Hiroko Uchida Akio Murakami Yoshiki Nakajima Makio Yokono Seiji Akimoto Naoshi Dohmae Koji Yonekura Jian-Ren Shen |
| author_facet | Koji Kato Tasuku Hamaguchi Ryo Nagao Keisuke Kawakami Yoshifumi Ueno Takehiro Suzuki Hiroko Uchida Akio Murakami Yoshiki Nakajima Makio Yokono Seiji Akimoto Naoshi Dohmae Koji Yonekura Jian-Ren Shen |
| author_sort | Koji Kato |
| collection | DOAJ |
| description | Photosystem I (PSI) is a multi-subunit pigment-protein complex that functions in light-harvesting and photochemical charge-separation reactions, followed by reduction of NADP to NADPH required for CO2 fixation in photosynthetic organisms. PSI from different photosynthetic organisms has a variety of chlorophylls (Chls), some of which are at lower-energy levels than its reaction center P700, a special pair of Chls, and are called low-energy Chls. However, the sites of low-energy Chls are still under debate. Here, we solved a 2.04-Å resolution structure of a PSI trimer by cryo-electron microscopy from a primordial cyanobacterium Gloeobacter violaceus PCC 7421, which has no low-energy Chls. The structure shows the absence of some subunits commonly found in other cyanobacteria, confirming the primordial nature of this cyanobacterium. Comparison with the known structures of PSI from other cyanobacteria and eukaryotic organisms reveals that one dimeric and one trimeric Chls are lacking in the Gloeobacter PSI. The dimeric and trimeric Chls are named Low1 and Low2, respectively. Low2 is missing in some cyanobacterial and eukaryotic PSIs, whereas Low1 is absent only in Gloeobacter. These findings provide insights into not only the identity of low-energy Chls in PSI, but also the evolutionary changes of low-energy Chls in oxyphototrophs. |
| first_indexed | 2024-04-12T12:13:01Z |
| format | Article |
| id | doaj.art-f7c608fd3f314f59ab9a16a2f9320b4a |
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| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T12:13:01Z |
| publishDate | 2022-04-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-f7c608fd3f314f59ab9a16a2f9320b4a2022-12-22T03:33:32ZengeLife Sciences Publications LtdeLife2050-084X2022-04-011110.7554/eLife.73990Structural basis for the absence of low-energy chlorophylls in a photosystem I trimer from Gloeobacter violaceusKoji Kato0Tasuku Hamaguchi1Ryo Nagao2https://orcid.org/0000-0001-8212-3001Keisuke Kawakami3Yoshifumi Ueno4Takehiro Suzuki5Hiroko Uchida6Akio Murakami7Yoshiki Nakajima8Makio Yokono9Seiji Akimoto10https://orcid.org/0000-0002-8951-8978Naoshi Dohmae11https://orcid.org/0000-0002-5242-9410Koji Yonekura12https://orcid.org/0000-0001-5520-4391Jian-Ren Shen13https://orcid.org/0000-0003-4471-8797Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, JapanBiostructural Mechanism Laboratory, RIKEN SPring-8 Center, Hyogo, JapanResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, JapanBiostructural Mechanism Laboratory, RIKEN SPring-8 Center, Hyogo, JapanGraduate School of Science, Kobe University, Hyogo, JapanBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Saitama, JapanResearch Center for Inland Seas, Kobe University, Hyogo, JapanGraduate School of Science, Kobe University, Hyogo, Japan; Research Center for Inland Seas, Kobe University, Hyogo, JapanResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, JapanInstitute of Low Temperature Science, Hokkaido University, Hokkaido, JapanGraduate School of Science, Kobe University, Hyogo, JapanBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Saitama, JapanBiostructural Mechanism Laboratory, RIKEN SPring-8 Center, Hyogo, Japan; Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Miyagi, Japan; Advanced Electron Microscope Development Unit, RIKEN-JEOL Collaboration Center, RIKEN Baton Zone Program, Hyogo, JapanResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, JapanPhotosystem I (PSI) is a multi-subunit pigment-protein complex that functions in light-harvesting and photochemical charge-separation reactions, followed by reduction of NADP to NADPH required for CO2 fixation in photosynthetic organisms. PSI from different photosynthetic organisms has a variety of chlorophylls (Chls), some of which are at lower-energy levels than its reaction center P700, a special pair of Chls, and are called low-energy Chls. However, the sites of low-energy Chls are still under debate. Here, we solved a 2.04-Å resolution structure of a PSI trimer by cryo-electron microscopy from a primordial cyanobacterium Gloeobacter violaceus PCC 7421, which has no low-energy Chls. The structure shows the absence of some subunits commonly found in other cyanobacteria, confirming the primordial nature of this cyanobacterium. Comparison with the known structures of PSI from other cyanobacteria and eukaryotic organisms reveals that one dimeric and one trimeric Chls are lacking in the Gloeobacter PSI. The dimeric and trimeric Chls are named Low1 and Low2, respectively. Low2 is missing in some cyanobacterial and eukaryotic PSIs, whereas Low1 is absent only in Gloeobacter. These findings provide insights into not only the identity of low-energy Chls in PSI, but also the evolutionary changes of low-energy Chls in oxyphototrophs.https://elifesciences.org/articles/73990photosystem Icryo-EMlow-energy ChlGloeobacter |
| spellingShingle | Koji Kato Tasuku Hamaguchi Ryo Nagao Keisuke Kawakami Yoshifumi Ueno Takehiro Suzuki Hiroko Uchida Akio Murakami Yoshiki Nakajima Makio Yokono Seiji Akimoto Naoshi Dohmae Koji Yonekura Jian-Ren Shen Structural basis for the absence of low-energy chlorophylls in a photosystem I trimer from Gloeobacter violaceus eLife photosystem I cryo-EM low-energy Chl Gloeobacter |
| title | Structural basis for the absence of low-energy chlorophylls in a photosystem I trimer from Gloeobacter violaceus |
| title_full | Structural basis for the absence of low-energy chlorophylls in a photosystem I trimer from Gloeobacter violaceus |
| title_fullStr | Structural basis for the absence of low-energy chlorophylls in a photosystem I trimer from Gloeobacter violaceus |
| title_full_unstemmed | Structural basis for the absence of low-energy chlorophylls in a photosystem I trimer from Gloeobacter violaceus |
| title_short | Structural basis for the absence of low-energy chlorophylls in a photosystem I trimer from Gloeobacter violaceus |
| title_sort | structural basis for the absence of low energy chlorophylls in a photosystem i trimer from gloeobacter violaceus |
| topic | photosystem I cryo-EM low-energy Chl Gloeobacter |
| url | https://elifesciences.org/articles/73990 |
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