Structural insight into light harvesting for photosystem II in green algae
Green algae and plants rely on light-harvesting complex II (LHCII) to collect photon energy for oxygenic photosynthesis. In Chlamydomonas reinhardtii , LHCII molecules associate with photosystem II (PSII) to form various supercomplexes, including the C 2 S 2 M 2 L 2 type, which is the largest PSII–L...
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creator | Sheng, Xin Watanabe, Akimasa Li, Anjie Kim, Eunchul Song, Chihong Murata, Kazuyoshi Song, Danfeng Minagawa, Jun Liu, Zhenfeng |
description | Green algae and plants rely on light-harvesting complex II (LHCII) to collect photon energy for oxygenic photosynthesis. In
Chlamydomonas reinhardtii
, LHCII molecules associate with photosystem II (PSII) to form various supercomplexes, including the C
2
S
2
M
2
L
2
type, which is the largest PSII–LHCII supercomplex in algae and plants that is presently known. Here, we report high-resolution cryo-electron microscopy (cryo-EM) maps and structural models of the C
2
S
2
M
2
L
2
and C
2
S
2
supercomplexes from
C. reinhardtii
. The C
2
S
2
supercomplex contains an LhcbM1–LhcbM2/7–LhcbM3 heterotrimer in the strongly associated LHCII, and the LhcbM1 subunit assembles with CP43 through two interfacial galactolipid molecules. The loosely and moderately associated LHCII trimers interact closely with the minor antenna complex CP29 to form an intricate subcomplex bound to CP47 in the C
2
S
2
M
2
L
2
supercomplex. A notable direct pathway is established for energy transfer from the loosely associated LHCII to the PSII reaction centre, as well as several indirect routes. Structure-based computational analysis on the excitation energy transfer within the two supercomplexes provides detailed mechanistic insights into the light-harvesting process in green algae.
High-resolution cryo-EM structures of
Chlamydomonas
light-harvesting complex II (LHCII)–photosystem II (PSII) supercomplexes show loosely and moderately associated LHCIIs forming multiple pathways for energy transfer to PSII reaction centres. |
doi_str_mv | 10.1038/s41477-019-0543-4 |
format | Article |
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Chlamydomonas reinhardtii
, LHCII molecules associate with photosystem II (PSII) to form various supercomplexes, including the C
2
S
2
M
2
L
2
type, which is the largest PSII–LHCII supercomplex in algae and plants that is presently known. Here, we report high-resolution cryo-electron microscopy (cryo-EM) maps and structural models of the C
2
S
2
M
2
L
2
and C
2
S
2
supercomplexes from
C. reinhardtii
. The C
2
S
2
supercomplex contains an LhcbM1–LhcbM2/7–LhcbM3 heterotrimer in the strongly associated LHCII, and the LhcbM1 subunit assembles with CP43 through two interfacial galactolipid molecules. The loosely and moderately associated LHCII trimers interact closely with the minor antenna complex CP29 to form an intricate subcomplex bound to CP47 in the C
2
S
2
M
2
L
2
supercomplex. A notable direct pathway is established for energy transfer from the loosely associated LHCII to the PSII reaction centre, as well as several indirect routes. Structure-based computational analysis on the excitation energy transfer within the two supercomplexes provides detailed mechanistic insights into the light-harvesting process in green algae.
High-resolution cryo-EM structures of
Chlamydomonas
light-harvesting complex II (LHCII)–photosystem II (PSII) supercomplexes show loosely and moderately associated LHCIIs forming multiple pathways for energy transfer to PSII reaction centres.</description><identifier>ISSN: 2055-0278</identifier><identifier>EISSN: 2055-0278</identifier><identifier>DOI: 10.1038/s41477-019-0543-4</identifier><identifier>PMID: 31768031</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>101/28 ; 631/1647/2258/1258/1259 ; 631/449/1734/2076 ; 82/83 ; Algae ; Aquatic plants ; Biomedical and Life Sciences ; Chlamydomonas reinhardtii - chemistry ; Chlamydomonas reinhardtii - genetics ; Chlamydomonas reinhardtii - metabolism ; Chlamydomonas reinhardtii - radiation effects ; Chlorophyll - metabolism ; Cryoelectron Microscopy ; Energy Transfer ; Life Sciences ; Light ; Light-harvesting complex ; Light-Harvesting Protein Complexes - genetics ; Light-Harvesting Protein Complexes - metabolism ; Models, Molecular ; Photosynthesis ; Photosystem II ; Photosystem II Protein Complex - chemistry ; Photosystem II Protein Complex - genetics ; Photosystem II Protein Complex - metabolism ; Plant Proteins - chemistry ; Plant Proteins - genetics ; Plant Proteins - metabolism ; Plant Sciences ; Protein Binding</subject><ispartof>Nature plants, 2019-12, Vol.5 (12), p.1320-1330</ispartof><rights>The Author(s), under exclusive licence to Springer Nature Limited 2019</rights><rights>Copyright Nature Publishing Group Dec 2019</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c372t-d3f2243748313536cb043cfa16202d47b8951e7edf7481d7de1ff46a155da3503</citedby><cites>FETCH-LOGICAL-c372t-d3f2243748313536cb043cfa16202d47b8951e7edf7481d7de1ff46a155da3503</cites><orcidid>0000-0001-6068-1328 ; 0000-0001-9446-3652 ; 0000-0001-8628-4267 ; 0000-0002-3028-3203</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/s41477-019-0543-4$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/s41477-019-0543-4$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,778,782,27907,27908,41471,42540,51302</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31768031$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sheng, Xin</creatorcontrib><creatorcontrib>Watanabe, Akimasa</creatorcontrib><creatorcontrib>Li, Anjie</creatorcontrib><creatorcontrib>Kim, Eunchul</creatorcontrib><creatorcontrib>Song, Chihong</creatorcontrib><creatorcontrib>Murata, Kazuyoshi</creatorcontrib><creatorcontrib>Song, Danfeng</creatorcontrib><creatorcontrib>Minagawa, Jun</creatorcontrib><creatorcontrib>Liu, Zhenfeng</creatorcontrib><title>Structural insight into light harvesting for photosystem II in green algae</title><title>Nature plants</title><addtitle>Nat. Plants</addtitle><addtitle>Nat Plants</addtitle><description>Green algae and plants rely on light-harvesting complex II (LHCII) to collect photon energy for oxygenic photosynthesis. In
Chlamydomonas reinhardtii
, LHCII molecules associate with photosystem II (PSII) to form various supercomplexes, including the C
2
S
2
M
2
L
2
type, which is the largest PSII–LHCII supercomplex in algae and plants that is presently known. Here, we report high-resolution cryo-electron microscopy (cryo-EM) maps and structural models of the C
2
S
2
M
2
L
2
and C
2
S
2
supercomplexes from
C. reinhardtii
. The C
2
S
2
supercomplex contains an LhcbM1–LhcbM2/7–LhcbM3 heterotrimer in the strongly associated LHCII, and the LhcbM1 subunit assembles with CP43 through two interfacial galactolipid molecules. The loosely and moderately associated LHCII trimers interact closely with the minor antenna complex CP29 to form an intricate subcomplex bound to CP47 in the C
2
S
2
M
2
L
2
supercomplex. A notable direct pathway is established for energy transfer from the loosely associated LHCII to the PSII reaction centre, as well as several indirect routes. Structure-based computational analysis on the excitation energy transfer within the two supercomplexes provides detailed mechanistic insights into the light-harvesting process in green algae.
High-resolution cryo-EM structures of
Chlamydomonas
light-harvesting complex II (LHCII)–photosystem II (PSII) supercomplexes show loosely and moderately associated LHCIIs forming multiple pathways for energy transfer to PSII reaction centres.</description><subject>101/28</subject><subject>631/1647/2258/1258/1259</subject><subject>631/449/1734/2076</subject><subject>82/83</subject><subject>Algae</subject><subject>Aquatic plants</subject><subject>Biomedical and Life Sciences</subject><subject>Chlamydomonas reinhardtii - chemistry</subject><subject>Chlamydomonas reinhardtii - genetics</subject><subject>Chlamydomonas reinhardtii - metabolism</subject><subject>Chlamydomonas reinhardtii - radiation effects</subject><subject>Chlorophyll - metabolism</subject><subject>Cryoelectron Microscopy</subject><subject>Energy Transfer</subject><subject>Life Sciences</subject><subject>Light</subject><subject>Light-harvesting complex</subject><subject>Light-Harvesting Protein Complexes - genetics</subject><subject>Light-Harvesting Protein Complexes - metabolism</subject><subject>Models, Molecular</subject><subject>Photosynthesis</subject><subject>Photosystem II</subject><subject>Photosystem II Protein Complex - chemistry</subject><subject>Photosystem II Protein Complex - genetics</subject><subject>Photosystem II Protein Complex - metabolism</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - metabolism</subject><subject>Plant Sciences</subject><subject>Protein Binding</subject><issn>2055-0278</issn><issn>2055-0278</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>AFKRA</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><recordid>eNp1kF1LwzAUhoMoTuZ-gDdS8Mab6slX013K8GMy8EK9DlmbdB1tM5NU2L83s_MDwatzIE_e8_IgdIbhCgPNrz3DTIgU8DQFzmjKDtAJAc5TICI__LWP0MT7NQBgwTnN4BiNKBZZDhSfoMfn4Poi9E41Sd35ulqFOINNms91pdy79qHuqsRYl2xWNli_9UG3yXwewaRyWneJaiqlT9GRUY3Xk_0co9e725fZQ7p4up_PbhZpQQUJaUkNIYwKllNMY59iCYwWRuGMACmZWOZTjrXQpYkILkWpsTEsU5jzUlEOdIwuh9yNs299bCfb2he6aVSnbe8loTgXZJrHI2N08Qdd2951sV2kCAUhAHik8EAVznrvtJEbV7fKbSUGuXMtB9cyupY713KXfL5P7petLr9_fJmNABkAH5-6Sruf0_-nfgCudYee</recordid><startdate>20191201</startdate><enddate>20191201</enddate><creator>Sheng, Xin</creator><creator>Watanabe, Akimasa</creator><creator>Li, Anjie</creator><creator>Kim, Eunchul</creator><creator>Song, Chihong</creator><creator>Murata, Kazuyoshi</creator><creator>Song, Danfeng</creator><creator>Minagawa, Jun</creator><creator>Liu, Zhenfeng</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SN</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>HCIFZ</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-6068-1328</orcidid><orcidid>https://orcid.org/0000-0001-9446-3652</orcidid><orcidid>https://orcid.org/0000-0001-8628-4267</orcidid><orcidid>https://orcid.org/0000-0002-3028-3203</orcidid></search><sort><creationdate>20191201</creationdate><title>Structural insight into light harvesting for photosystem II in green algae</title><author>Sheng, Xin ; Watanabe, Akimasa ; Li, Anjie ; Kim, Eunchul ; Song, Chihong ; Murata, Kazuyoshi ; Song, Danfeng ; Minagawa, Jun ; Liu, Zhenfeng</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c372t-d3f2243748313536cb043cfa16202d47b8951e7edf7481d7de1ff46a155da3503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>101/28</topic><topic>631/1647/2258/1258/1259</topic><topic>631/449/1734/2076</topic><topic>82/83</topic><topic>Algae</topic><topic>Aquatic plants</topic><topic>Biomedical and Life Sciences</topic><topic>Chlamydomonas reinhardtii - chemistry</topic><topic>Chlamydomonas reinhardtii - genetics</topic><topic>Chlamydomonas reinhardtii - metabolism</topic><topic>Chlamydomonas reinhardtii - radiation effects</topic><topic>Chlorophyll - metabolism</topic><topic>Cryoelectron Microscopy</topic><topic>Energy Transfer</topic><topic>Life Sciences</topic><topic>Light</topic><topic>Light-harvesting complex</topic><topic>Light-Harvesting Protein Complexes - genetics</topic><topic>Light-Harvesting Protein Complexes - metabolism</topic><topic>Models, Molecular</topic><topic>Photosynthesis</topic><topic>Photosystem II</topic><topic>Photosystem II Protein Complex - chemistry</topic><topic>Photosystem II Protein Complex - genetics</topic><topic>Photosystem II Protein Complex - metabolism</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - metabolism</topic><topic>Plant Sciences</topic><topic>Protein Binding</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sheng, Xin</creatorcontrib><creatorcontrib>Watanabe, Akimasa</creatorcontrib><creatorcontrib>Li, Anjie</creatorcontrib><creatorcontrib>Kim, Eunchul</creatorcontrib><creatorcontrib>Song, Chihong</creatorcontrib><creatorcontrib>Murata, Kazuyoshi</creatorcontrib><creatorcontrib>Song, Danfeng</creatorcontrib><creatorcontrib>Minagawa, Jun</creatorcontrib><creatorcontrib>Liu, Zhenfeng</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Ecology Abstracts</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>SciTech Premium Collection</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>MEDLINE - Academic</collection><jtitle>Nature plants</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sheng, Xin</au><au>Watanabe, Akimasa</au><au>Li, Anjie</au><au>Kim, Eunchul</au><au>Song, Chihong</au><au>Murata, Kazuyoshi</au><au>Song, Danfeng</au><au>Minagawa, Jun</au><au>Liu, Zhenfeng</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural insight into light harvesting for photosystem II in green algae</atitle><jtitle>Nature plants</jtitle><stitle>Nat. Plants</stitle><addtitle>Nat Plants</addtitle><date>2019-12-01</date><risdate>2019</risdate><volume>5</volume><issue>12</issue><spage>1320</spage><epage>1330</epage><pages>1320-1330</pages><issn>2055-0278</issn><eissn>2055-0278</eissn><abstract>Green algae and plants rely on light-harvesting complex II (LHCII) to collect photon energy for oxygenic photosynthesis. In
Chlamydomonas reinhardtii
, LHCII molecules associate with photosystem II (PSII) to form various supercomplexes, including the C
2
S
2
M
2
L
2
type, which is the largest PSII–LHCII supercomplex in algae and plants that is presently known. Here, we report high-resolution cryo-electron microscopy (cryo-EM) maps and structural models of the C
2
S
2
M
2
L
2
and C
2
S
2
supercomplexes from
C. reinhardtii
. The C
2
S
2
supercomplex contains an LhcbM1–LhcbM2/7–LhcbM3 heterotrimer in the strongly associated LHCII, and the LhcbM1 subunit assembles with CP43 through two interfacial galactolipid molecules. The loosely and moderately associated LHCII trimers interact closely with the minor antenna complex CP29 to form an intricate subcomplex bound to CP47 in the C
2
S
2
M
2
L
2
supercomplex. A notable direct pathway is established for energy transfer from the loosely associated LHCII to the PSII reaction centre, as well as several indirect routes. Structure-based computational analysis on the excitation energy transfer within the two supercomplexes provides detailed mechanistic insights into the light-harvesting process in green algae.
High-resolution cryo-EM structures of
Chlamydomonas
light-harvesting complex II (LHCII)–photosystem II (PSII) supercomplexes show loosely and moderately associated LHCIIs forming multiple pathways for energy transfer to PSII reaction centres.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>31768031</pmid><doi>10.1038/s41477-019-0543-4</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0001-6068-1328</orcidid><orcidid>https://orcid.org/0000-0001-9446-3652</orcidid><orcidid>https://orcid.org/0000-0001-8628-4267</orcidid><orcidid>https://orcid.org/0000-0002-3028-3203</orcidid></addata></record> |
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subjects | 101/28 631/1647/2258/1258/1259 631/449/1734/2076 82/83 Algae Aquatic plants Biomedical and Life Sciences Chlamydomonas reinhardtii - chemistry Chlamydomonas reinhardtii - genetics Chlamydomonas reinhardtii - metabolism Chlamydomonas reinhardtii - radiation effects Chlorophyll - metabolism Cryoelectron Microscopy Energy Transfer Life Sciences Light Light-harvesting complex Light-Harvesting Protein Complexes - genetics Light-Harvesting Protein Complexes - metabolism Models, Molecular Photosynthesis Photosystem II Photosystem II Protein Complex - chemistry Photosystem II Protein Complex - genetics Photosystem II Protein Complex - metabolism Plant Proteins - chemistry Plant Proteins - genetics Plant Proteins - metabolism Plant Sciences Protein Binding |
title | Structural insight into light harvesting for photosystem II in green algae |
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