Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas
The pyrenoid is a subcellular microcompartment in which algae sequester the primary carboxylase, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). The pyrenoid is associated with a CO ₂-concentrating mechanism (CCM), which improves the operating efficiency of carbon assimilation and overcom...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2012-11, Vol.109 (47), p.19474-19479 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Meyer, Moritz T Genkov, Todor Skepper, Jeremy N Jouhet, Juliette Mitchell, Madeline C Spreitzer, Robert J Griffiths, Howard |
| description | The pyrenoid is a subcellular microcompartment in which algae sequester the primary carboxylase, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). The pyrenoid is associated with a CO ₂-concentrating mechanism (CCM), which improves the operating efficiency of carbon assimilation and overcomes diffusive limitations in aquatic photosynthesis. Using the model alga Chlamydomonas reinhardtii , we show that pyrenoid formation, Rubisco aggregation, and CCM activity relate to discrete regions of the Rubisco small subunit (SSU). Specifically, pyrenoid occurrence was shown to be conditioned by the amino acid composition of two surface-exposed α-helices of the SSU: higher plant-like helices knock out the pyrenoid, whereas native algal helices establish a pyrenoid. We have also established that pyrenoid integrity was essential for the operation of an active CCM. With the algal CCM being functionally analogous to the terrestrial C ₄ pathway in higher plants, such insights may offer a route toward transforming algal and higher plant productivity for the future. |
| doi_str_mv | 10.1073/pnas.1210993109 |
| format | Article |
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The pyrenoid is associated with a CO ₂-concentrating mechanism (CCM), which improves the operating efficiency of carbon assimilation and overcomes diffusive limitations in aquatic photosynthesis. Using the model alga Chlamydomonas reinhardtii , we show that pyrenoid formation, Rubisco aggregation, and CCM activity relate to discrete regions of the Rubisco small subunit (SSU). Specifically, pyrenoid occurrence was shown to be conditioned by the amino acid composition of two surface-exposed α-helices of the SSU: higher plant-like helices knock out the pyrenoid, whereas native algal helices establish a pyrenoid. We have also established that pyrenoid integrity was essential for the operation of an active CCM. With the algal CCM being functionally analogous to the terrestrial C ₄ pathway in higher plants, such insights may offer a route toward transforming algal and higher plant productivity for the future.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1210993109</identifier><identifier>PMID: 23112177</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Algae ; amino acid composition ; Amino Acid Sequence ; Amino acids ; Autotrophic Processes - drug effects ; Biochemistry, Molecular Biology ; Biological Sciences ; carbon ; Carbon - metabolism ; Carbon Dioxide - pharmacology ; Chlamydomonas - drug effects ; Chlamydomonas - enzymology ; Chlamydomonas - growth & development ; Chlamydomonas - ultrastructure ; Chlamydomonas reinhardtii ; Chloroplasts ; Enzymes ; Gene Deletion ; Hybridity ; Kinetics ; Life Sciences ; Molecular Sequence Data ; Organelles - metabolism ; Organelles - ultrastructure ; Oxygen - metabolism ; Phenotype ; Photosynthesis ; Photosynthesis - drug effects ; Plants ; Protein Structure, Secondary ; ribulose-bisphosphate carboxylase ; Ribulose-Bisphosphate Carboxylase - chemistry ; Ribulose-Bisphosphate Carboxylase - metabolism ; Spinach ; Spinacia oleracea - drug effects ; Spinacia oleracea - enzymology ; Structure-Activity Relationship ; Thylakoids</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2012-11, Vol.109 (47), p.19474-19479</ispartof><rights>copyright © 1993-2008 National Academy of Sciences of the United States of America</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c531t-4d06fe91307633d4a20460c4a2b48454a269574708f4af1a298ba1b66a667a573</citedby><cites>FETCH-LOGICAL-c531t-4d06fe91307633d4a20460c4a2b48454a269574708f4af1a298ba1b66a667a573</cites><orcidid>0000-0002-4402-2194</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/109/47.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41830233$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41830233$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53770,53772,57996,58229</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23112177$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00750796$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Meyer, Moritz T</creatorcontrib><creatorcontrib>Genkov, Todor</creatorcontrib><creatorcontrib>Skepper, Jeremy N</creatorcontrib><creatorcontrib>Jouhet, Juliette</creatorcontrib><creatorcontrib>Mitchell, Madeline C</creatorcontrib><creatorcontrib>Spreitzer, Robert J</creatorcontrib><creatorcontrib>Griffiths, Howard</creatorcontrib><title>Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The pyrenoid is a subcellular microcompartment in which algae sequester the primary carboxylase, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). The pyrenoid is associated with a CO ₂-concentrating mechanism (CCM), which improves the operating efficiency of carbon assimilation and overcomes diffusive limitations in aquatic photosynthesis. Using the model alga Chlamydomonas reinhardtii , we show that pyrenoid formation, Rubisco aggregation, and CCM activity relate to discrete regions of the Rubisco small subunit (SSU). Specifically, pyrenoid occurrence was shown to be conditioned by the amino acid composition of two surface-exposed α-helices of the SSU: higher plant-like helices knock out the pyrenoid, whereas native algal helices establish a pyrenoid. We have also established that pyrenoid integrity was essential for the operation of an active CCM. With the algal CCM being functionally analogous to the terrestrial C ₄ pathway in higher plants, such insights may offer a route toward transforming algal and higher plant productivity for the future.</description><subject>Algae</subject><subject>amino acid composition</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Autotrophic Processes - drug effects</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological Sciences</subject><subject>carbon</subject><subject>Carbon - metabolism</subject><subject>Carbon Dioxide - pharmacology</subject><subject>Chlamydomonas - drug effects</subject><subject>Chlamydomonas - enzymology</subject><subject>Chlamydomonas - growth & development</subject><subject>Chlamydomonas - ultrastructure</subject><subject>Chlamydomonas reinhardtii</subject><subject>Chloroplasts</subject><subject>Enzymes</subject><subject>Gene Deletion</subject><subject>Hybridity</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Molecular Sequence Data</subject><subject>Organelles - metabolism</subject><subject>Organelles - ultrastructure</subject><subject>Oxygen - metabolism</subject><subject>Phenotype</subject><subject>Photosynthesis</subject><subject>Photosynthesis - drug effects</subject><subject>Plants</subject><subject>Protein Structure, Secondary</subject><subject>ribulose-bisphosphate carboxylase</subject><subject>Ribulose-Bisphosphate Carboxylase - chemistry</subject><subject>Ribulose-Bisphosphate Carboxylase - metabolism</subject><subject>Spinach</subject><subject>Spinacia oleracea - drug effects</subject><subject>Spinacia oleracea - enzymology</subject><subject>Structure-Activity Relationship</subject><subject>Thylakoids</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkcFu1DAQhi0EokvhzAnIEQ5pZ2zHji9I1Qoo0kpIQM-WkzhdV0682EmlfSxehGfCqyxb4DIjeb7_99g_IS8RLhAku9yNJl0gRVCK5fKIrHLFUnAFj8kKgMqy5pSfkWcp3QGAqmp4Ss4owyySckU2X-fGpTYUaTDel2lu5tFNxa-f5dZ619pUtGGcYvDFbh_tGFxX9CEOZnJhLNxYrLfeDPsuDCFv8pw86Y1P9sWxn5Objx--r6_LzZdPn9dXm7KtGE4l70D0ViEDKRjruKHABbS5N7zmVe5CVZJLqHtuejRU1Y3BRggjhDSVZOfk_eK7m5vBdq3NGxqvd9ENJu51ME7_OxndVt-Ge80qRKjrbPBuMdj-J7u-2ujDGYCsQCpxj5l9e7wshh-zTZMe8odZ781ow5w01sCQU8pYRi8XtI0hpWj7kzeCPuSlD3nph7yy4vXfLznxfwLKQHEEDsoHO6W51Ki45Bl5tSB3aQrxxHCsGSxbvVnmvQna3EaX9M03CigAcgRMKvYbTkqurA</recordid><startdate>20121120</startdate><enddate>20121120</enddate><creator>Meyer, Moritz T</creator><creator>Genkov, Todor</creator><creator>Skepper, Jeremy N</creator><creator>Jouhet, Juliette</creator><creator>Mitchell, Madeline C</creator><creator>Spreitzer, Robert J</creator><creator>Griffiths, Howard</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</scope><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>7S9</scope><scope>L.6</scope><scope>1XC</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-4402-2194</orcidid></search><sort><creationdate>20121120</creationdate><title>Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas</title><author>Meyer, Moritz T ; Genkov, Todor ; Skepper, Jeremy N ; Jouhet, Juliette ; Mitchell, Madeline C ; Spreitzer, Robert J ; Griffiths, Howard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c531t-4d06fe91307633d4a20460c4a2b48454a269574708f4af1a298ba1b66a667a573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Algae</topic><topic>amino acid composition</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Autotrophic Processes - drug effects</topic><topic>Biochemistry, Molecular Biology</topic><topic>Biological Sciences</topic><topic>carbon</topic><topic>Carbon - metabolism</topic><topic>Carbon Dioxide - pharmacology</topic><topic>Chlamydomonas - drug effects</topic><topic>Chlamydomonas - enzymology</topic><topic>Chlamydomonas - growth & development</topic><topic>Chlamydomonas - ultrastructure</topic><topic>Chlamydomonas reinhardtii</topic><topic>Chloroplasts</topic><topic>Enzymes</topic><topic>Gene Deletion</topic><topic>Hybridity</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Molecular Sequence Data</topic><topic>Organelles - metabolism</topic><topic>Organelles - ultrastructure</topic><topic>Oxygen - metabolism</topic><topic>Phenotype</topic><topic>Photosynthesis</topic><topic>Photosynthesis - drug effects</topic><topic>Plants</topic><topic>Protein Structure, Secondary</topic><topic>ribulose-bisphosphate carboxylase</topic><topic>Ribulose-Bisphosphate Carboxylase - chemistry</topic><topic>Ribulose-Bisphosphate Carboxylase - metabolism</topic><topic>Spinach</topic><topic>Spinacia oleracea - drug effects</topic><topic>Spinacia oleracea - enzymology</topic><topic>Structure-Activity Relationship</topic><topic>Thylakoids</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Meyer, Moritz T</creatorcontrib><creatorcontrib>Genkov, Todor</creatorcontrib><creatorcontrib>Skepper, Jeremy N</creatorcontrib><creatorcontrib>Jouhet, Juliette</creatorcontrib><creatorcontrib>Mitchell, Madeline C</creatorcontrib><creatorcontrib>Spreitzer, Robert J</creatorcontrib><creatorcontrib>Griffiths, Howard</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Meyer, Moritz T</au><au>Genkov, Todor</au><au>Skepper, Jeremy N</au><au>Jouhet, Juliette</au><au>Mitchell, Madeline C</au><au>Spreitzer, Robert J</au><au>Griffiths, Howard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2012-11-20</date><risdate>2012</risdate><volume>109</volume><issue>47</issue><spage>19474</spage><epage>19479</epage><pages>19474-19479</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The pyrenoid is a subcellular microcompartment in which algae sequester the primary carboxylase, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). The pyrenoid is associated with a CO ₂-concentrating mechanism (CCM), which improves the operating efficiency of carbon assimilation and overcomes diffusive limitations in aquatic photosynthesis. Using the model alga Chlamydomonas reinhardtii , we show that pyrenoid formation, Rubisco aggregation, and CCM activity relate to discrete regions of the Rubisco small subunit (SSU). Specifically, pyrenoid occurrence was shown to be conditioned by the amino acid composition of two surface-exposed α-helices of the SSU: higher plant-like helices knock out the pyrenoid, whereas native algal helices establish a pyrenoid. We have also established that pyrenoid integrity was essential for the operation of an active CCM. 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| subjects | Algae amino acid composition Amino Acid Sequence Amino acids Autotrophic Processes - drug effects Biochemistry, Molecular Biology Biological Sciences carbon Carbon - metabolism Carbon Dioxide - pharmacology Chlamydomonas - drug effects Chlamydomonas - enzymology Chlamydomonas - growth & development Chlamydomonas - ultrastructure Chlamydomonas reinhardtii Chloroplasts Enzymes Gene Deletion Hybridity Kinetics Life Sciences Molecular Sequence Data Organelles - metabolism Organelles - ultrastructure Oxygen - metabolism Phenotype Photosynthesis Photosynthesis - drug effects Plants Protein Structure, Secondary ribulose-bisphosphate carboxylase Ribulose-Bisphosphate Carboxylase - chemistry Ribulose-Bisphosphate Carboxylase - metabolism Spinach Spinacia oleracea - drug effects Spinacia oleracea - enzymology Structure-Activity Relationship Thylakoids |
| title | Rubisco small-subunit α-helices control pyrenoid formation in Chlamydomonas |
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