Identification of a protein required for recovery of full antenna capacity in OCP-related photoprotective mechanism in cyanobacteria
High light can be lethal for photosynthetic organisms. Similar to plants, most cyanobacteria protect themselves from high irradiance by increasing thermal dissipation of excess absorbed energy. The photoactive soluble orange carotenoid protein (OCP) is essential for the triggering of this photoprote...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2010-06, Vol.107 (25), p.11620-11625 |
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creator | Boulay, Clémence Wilson, Adjélé D'Haene, Sandrine Kirilovsky, Diana Haselkorn, Robert |
description | High light can be lethal for photosynthetic organisms. Similar to plants, most cyanobacteria protect themselves from high irradiance by increasing thermal dissipation of excess absorbed energy. The photoactive soluble orange carotenoid protein (OCP) is essential for the triggering of this photoprotective mechanism. Light induces structural changes in the carotenoid and the protein, leading to the formation of a red active form. Through targeted gene interruption we have now identified a protein that mediates the recovery of the full antenna capacity when irradiance decreases. In Synechocystis PCC 6803, this protein, which we called the fluorescence recovery protein (FRP), is encoded by the slr1964 gene. Homologues of this gene are present in all of the OCP-containing strains. The FRP is a 14-kDa protein, strongly attached to the membrane, which interacts with the active red form of the OCP. In vitro this interaction greatly accelerates the conversion of the red OCP form to the orange form. We propose that in vivo, FRP plays a key role in removing the red OCP from the phycobilisome and in the conversion of the free red OCP to the orange inactive form. The discovery of FRP and its characterization are essential elements in the understanding of the OCP-related photoprotective mechanism in cyanobacteria. |
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Similar to plants, most cyanobacteria protect themselves from high irradiance by increasing thermal dissipation of excess absorbed energy. The photoactive soluble orange carotenoid protein (OCP) is essential for the triggering of this photoprotective mechanism. Light induces structural changes in the carotenoid and the protein, leading to the formation of a red active form. Through targeted gene interruption we have now identified a protein that mediates the recovery of the full antenna capacity when irradiance decreases. In Synechocystis PCC 6803, this protein, which we called the fluorescence recovery protein (FRP), is encoded by the slr1964 gene. Homologues of this gene are present in all of the OCP-containing strains. The FRP is a 14-kDa protein, strongly attached to the membrane, which interacts with the active red form of the OCP. In vitro this interaction greatly accelerates the conversion of the red OCP form to the orange form. We propose that in vivo, FRP plays a key role in removing the red OCP from the phycobilisome and in the conversion of the free red OCP to the orange inactive form. The discovery of FRP and its characterization are essential elements in the understanding of the OCP-related photoprotective mechanism in cyanobacteria.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1002912107</identifier><identifier>PMID: 20534537</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Amino Acid Sequence ; Antibodies ; Bacteria ; Bacterial Proteins - metabolism ; Biochemistry, Molecular Biology ; Biological Sciences ; Carotenoids ; Carotenoids - metabolism ; Carrier Proteins - genetics ; Carrier Proteins - physiology ; Cyanobacteria ; Cyanobacteria - metabolism ; Fluorescence ; Gene expression ; Genes ; Histidine - chemistry ; Irradiance ; Kinetics ; Life Sciences ; Light ; Membrane Proteins - genetics ; Membrane Proteins - physiology ; Membranes ; Messenger RNA ; Models, Biological ; Molecular Sequence Data ; Mutation ; Photochemistry - methods ; Photosynthesis ; Phycobilisome ; Phycobilisomes - metabolism ; Pigments ; Plants ; Proteins ; Synechocystis ; Synechocystis - metabolism</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2010-06, Vol.107 (25), p.11620-11625</ispartof><rights>copyright © 1993-2008 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Jun 22, 2010</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-c598t-8fd36aad46281d88938f2d378b851e8093f0f92f5a11f3467bc245ef39a352c23</citedby><cites>FETCH-LOGICAL-c598t-8fd36aad46281d88938f2d378b851e8093f0f92f5a11f3467bc245ef39a352c23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/107/25.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/20724117$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/20724117$$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/20534537$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00554176$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Boulay, Clémence</creatorcontrib><creatorcontrib>Wilson, Adjélé</creatorcontrib><creatorcontrib>D'Haene, Sandrine</creatorcontrib><creatorcontrib>Kirilovsky, Diana</creatorcontrib><creatorcontrib>Haselkorn, Robert</creatorcontrib><title>Identification of a protein required for recovery of full antenna capacity in OCP-related photoprotective mechanism in cyanobacteria</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>High light can be lethal for photosynthetic organisms. Similar to plants, most cyanobacteria protect themselves from high irradiance by increasing thermal dissipation of excess absorbed energy. The photoactive soluble orange carotenoid protein (OCP) is essential for the triggering of this photoprotective mechanism. Light induces structural changes in the carotenoid and the protein, leading to the formation of a red active form. Through targeted gene interruption we have now identified a protein that mediates the recovery of the full antenna capacity when irradiance decreases. In Synechocystis PCC 6803, this protein, which we called the fluorescence recovery protein (FRP), is encoded by the slr1964 gene. Homologues of this gene are present in all of the OCP-containing strains. The FRP is a 14-kDa protein, strongly attached to the membrane, which interacts with the active red form of the OCP. In vitro this interaction greatly accelerates the conversion of the red OCP form to the orange form. We propose that in vivo, FRP plays a key role in removing the red OCP from the phycobilisome and in the conversion of the free red OCP to the orange inactive form. The discovery of FRP and its characterization are essential elements in the understanding of the OCP-related photoprotective mechanism in cyanobacteria.</description><subject>Amino Acid Sequence</subject><subject>Antibodies</subject><subject>Bacteria</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological Sciences</subject><subject>Carotenoids</subject><subject>Carotenoids - metabolism</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - physiology</subject><subject>Cyanobacteria</subject><subject>Cyanobacteria - metabolism</subject><subject>Fluorescence</subject><subject>Gene expression</subject><subject>Genes</subject><subject>Histidine - chemistry</subject><subject>Irradiance</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Light</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - physiology</subject><subject>Membranes</subject><subject>Messenger RNA</subject><subject>Models, Biological</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Photochemistry - methods</subject><subject>Photosynthesis</subject><subject>Phycobilisome</subject><subject>Phycobilisomes - metabolism</subject><subject>Pigments</subject><subject>Plants</subject><subject>Proteins</subject><subject>Synechocystis</subject><subject>Synechocystis - metabolism</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkktvEzEUhUcIRENhzQo0YoNYDPVz7NkgVRHQSpHKAtbWjccmjib21PZEyp4fjoeEtnTFyvb1d87141TVa4w-YiToxeghlRkiHSal8KRaYNThpmUdelotSl00khF2Vr1IaYsQ6rhEz6szgjhlnIpF9eu6Nz476zRkF3wdbA31GEM2ztfR3E4umr62IZaFDnsTDzNip2GowWfjPdQaRtAuH-qiuFl-a6IZIBfRuAk5_LHS2e1NvTN6A96l3QzqA_iwBp1NdPCyemZhSObVaTyvfnz5_H151axuvl4vL1eN5p3MjbQ9bQF61hKJeyk7Ki3pqZBrybGRqKMW2Y5YDhhbylqx1oRxY2kHlBNN6Hn16eg7Tuud6XW5eYRBjdHtIB5UAKf-3fFuo36GvSKy40iKYvDhaLB5JLu6XKm5hhDnDIt2jwv7_tQshtvJpKx2LmkzDOBNmJISvPwAI-g_SEoZQoLRQr57RG7DFH15M8UJxpJIiQp0cYR0DClFY-9OipGaU6Pm1Kj71BTF24fvcsf_jUkB6hMwK-_thCJcYdySueubI7JNOcQHFoIwjAX9DZeT0yM</recordid><startdate>20100622</startdate><enddate>20100622</enddate><creator>Boulay, Clémence</creator><creator>Wilson, Adjélé</creator><creator>D'Haene, Sandrine</creator><creator>Kirilovsky, Diana</creator><creator>Haselkorn, Robert</creator><general>National Academy of Sciences</general><general>National Acad Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>1XC</scope><scope>5PM</scope></search><sort><creationdate>20100622</creationdate><title>Identification of a protein required for recovery of full antenna capacity in OCP-related photoprotective mechanism in cyanobacteria</title><author>Boulay, Clémence ; 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Similar to plants, most cyanobacteria protect themselves from high irradiance by increasing thermal dissipation of excess absorbed energy. The photoactive soluble orange carotenoid protein (OCP) is essential for the triggering of this photoprotective mechanism. Light induces structural changes in the carotenoid and the protein, leading to the formation of a red active form. Through targeted gene interruption we have now identified a protein that mediates the recovery of the full antenna capacity when irradiance decreases. In Synechocystis PCC 6803, this protein, which we called the fluorescence recovery protein (FRP), is encoded by the slr1964 gene. Homologues of this gene are present in all of the OCP-containing strains. The FRP is a 14-kDa protein, strongly attached to the membrane, which interacts with the active red form of the OCP. In vitro this interaction greatly accelerates the conversion of the red OCP form to the orange form. We propose that in vivo, FRP plays a key role in removing the red OCP from the phycobilisome and in the conversion of the free red OCP to the orange inactive form. The discovery of FRP and its characterization are essential elements in the understanding of the OCP-related photoprotective mechanism in cyanobacteria.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>20534537</pmid><doi>10.1073/pnas.1002912107</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Antibodies Bacteria Bacterial Proteins - metabolism Biochemistry, Molecular Biology Biological Sciences Carotenoids Carotenoids - metabolism Carrier Proteins - genetics Carrier Proteins - physiology Cyanobacteria Cyanobacteria - metabolism Fluorescence Gene expression Genes Histidine - chemistry Irradiance Kinetics Life Sciences Light Membrane Proteins - genetics Membrane Proteins - physiology Membranes Messenger RNA Models, Biological Molecular Sequence Data Mutation Photochemistry - methods Photosynthesis Phycobilisome Phycobilisomes - metabolism Pigments Plants Proteins Synechocystis Synechocystis - metabolism |
title | Identification of a protein required for recovery of full antenna capacity in OCP-related photoprotective mechanism in cyanobacteria |
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