Analysis of the chloroplast protein kinase Stt7 during state transitions
State transitions allow for the balancing of the light excitation energy between photosystem I and photosystem II and for optimal photosynthetic activity when photosynthetic organisms are subjected to changing light conditions. This process is regulated by the redox state of the plastoquinone pool t...
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description | State transitions allow for the balancing of the light excitation energy between photosystem I and photosystem II and for optimal photosynthetic activity when photosynthetic organisms are subjected to changing light conditions. This process is regulated by the redox state of the plastoquinone pool through the Stt7/STN7 protein kinase required for phosphorylation of the light-harvesting complex LHCII and for the reversible displacement of the mobile LHCII between the photosystems. We show that Stt7 is associated with photosynthetic complexes including LHCII, photosystem I, and the cytochrome b6f complex. Our data reveal that Stt7 acts in catalytic amounts. We also provide evidence that Stt7 contains a transmembrane region that separates its catalytic kinase domain on the stromal side from its N-terminal end in the thylakoid lumen with two conserved Cys that are critical for its activity and state transitions. On the basis of these data, we propose that the activity of Stt7 is regulated through its transmembrane domain and that a disulfide bond between the two lumen Cys is essential for its activity. The high-light-induced reduction of this bond may occur through a transthylakoid thiol-reducing pathway driven by the ferredoxin-thioredoxin system which is also required for cytochrome b6f assembly and heme biogenesis. |
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This process is regulated by the redox state of the plastoquinone pool through the Stt7/STN7 protein kinase required for phosphorylation of the light-harvesting complex LHCII and for the reversible displacement of the mobile LHCII between the photosystems. We show that Stt7 is associated with photosynthetic complexes including LHCII, photosystem I, and the cytochrome b6f complex. Our data reveal that Stt7 acts in catalytic amounts. We also provide evidence that Stt7 contains a transmembrane region that separates its catalytic kinase domain on the stromal side from its N-terminal end in the thylakoid lumen with two conserved Cys that are critical for its activity and state transitions. On the basis of these data, we propose that the activity of Stt7 is regulated through its transmembrane domain and that a disulfide bond between the two lumen Cys is essential for its activity. 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This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Lemeille S, Willig A, Depège-Fargeix N, Delessert C, Bassi R, et al. (2009) Analysis of the Chloroplast Protein Kinase Stt7 during State Transitions. 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This process is regulated by the redox state of the plastoquinone pool through the Stt7/STN7 protein kinase required for phosphorylation of the light-harvesting complex LHCII and for the reversible displacement of the mobile LHCII between the photosystems. We show that Stt7 is associated with photosynthetic complexes including LHCII, photosystem I, and the cytochrome b6f complex. Our data reveal that Stt7 acts in catalytic amounts. We also provide evidence that Stt7 contains a transmembrane region that separates its catalytic kinase domain on the stromal side from its N-terminal end in the thylakoid lumen with two conserved Cys that are critical for its activity and state transitions. On the basis of these data, we propose that the activity of Stt7 is regulated through its transmembrane domain and that a disulfide bond between the two lumen Cys is essential for its activity. The high-light-induced reduction of this bond may occur through a transthylakoid thiol-reducing pathway driven by the ferredoxin-thioredoxin system which is also required for cytochrome b6f assembly and heme biogenesis.</description><subject>Adaptation, Physiological</subject><subject>Algal Proteins - chemistry</subject><subject>Algal Proteins - physiology</subject><subject>Animals</subject><subject>Bands</subject><subject>Chlamydomonas - enzymology</subject><subject>Chlamydomonas - physiology</subject><subject>Chlorophyll</subject><subject>Chloroplasts</subject><subject>Chloroplasts - enzymology</subject><subject>Chloroplasts - physiology</subject><subject>Cytochrome b6f Complex - physiology</subject><subject>Kinases</subject><subject>Light</subject><subject>Light-Harvesting Protein Complexes - physiology</subject><subject>Phosphorylation</subject><subject>Photosynthesis</subject><subject>Photosynthesis - physiology</subject><subject>Photosystem I Protein Complex - physiology</subject><subject>Photosystem II Protein Complex - physiology</subject><subject>Plant Biology</subject><subject>Protein Conformation</subject><subject>Protein Kinases - chemistry</subject><subject>Protein Kinases - physiology</subject><subject>Proteins</subject><subject>Structure-Activity Relationship</subject><issn>1545-7885</issn><issn>1544-9173</issn><issn>1545-7885</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>DOA</sourceid><recordid>eNqFks1vFCEYxidGYz_0PzDKyduufH9cTJpG2yZNelDPhGFgl5UdRmCa9L-XdqfansoFAg-_933ePF33AcE1IgJ92aU5jyaupz6kNYJtUfaqO0aMspWQkr1-cj7qTkrZQYixwvJtd4QU5lBwdNxdnjXGXQkFJA_q1gG7jSmnKZpSwZRTdWEEv8NoigM_ahVgmHMYN6BUUx2o2Ywl1JDG8q57400s7v2yn3a_vn_7eX65ur65uDo_u15ZpkhdEQNp7zgiA-NOMiWw7E0PJcZcQMewMopxqKiHgxwsJXgwTkkqODGIeOjJaffpwJ1iKnoZQtGoOUNCNUhTXB0UQzI7PeWwN_lOJxP0w0XKG21yDTY6DXvMrRXeWuepb4V6pBTFRjLSGzGwxvq6VJv7vRusG5vl-Az6_GUMW71JtxpzBpu3Bvi8AHL6M7tS9T4U62I0o0tz0a1hpRBnLwoxbMNSlDchPQhtTqVk5_91g6C-T8bjUPR9MvSSjPbt41Mn_z8tUSB_AV0xt_0</recordid><startdate>20090301</startdate><enddate>20090301</enddate><creator>Lemeille, Sylvain</creator><creator>Willig, Adrian</creator><creator>Depège-Fargeix, Nathalie</creator><creator>Delessert, Christian</creator><creator>Bassi, Roberto</creator><creator>Rochaix, Jean-David</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>7ST</scope><scope>7U6</scope><scope>C1K</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><scope>CZG</scope></search><sort><creationdate>20090301</creationdate><title>Analysis of the chloroplast protein kinase Stt7 during state transitions</title><author>Lemeille, Sylvain ; Willig, Adrian ; Depège-Fargeix, Nathalie ; Delessert, Christian ; Bassi, Roberto ; Rochaix, Jean-David</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c593t-3a04be613d56e859728bab0822670e529a956094f0d8dc432dae984763a13f0f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Adaptation, Physiological</topic><topic>Algal Proteins - chemistry</topic><topic>Algal Proteins - physiology</topic><topic>Animals</topic><topic>Bands</topic><topic>Chlamydomonas - enzymology</topic><topic>Chlamydomonas - physiology</topic><topic>Chlorophyll</topic><topic>Chloroplasts</topic><topic>Chloroplasts - enzymology</topic><topic>Chloroplasts - physiology</topic><topic>Cytochrome b6f Complex - physiology</topic><topic>Kinases</topic><topic>Light</topic><topic>Light-Harvesting Protein Complexes - physiology</topic><topic>Phosphorylation</topic><topic>Photosynthesis</topic><topic>Photosynthesis - physiology</topic><topic>Photosystem I Protein Complex - physiology</topic><topic>Photosystem II Protein Complex - physiology</topic><topic>Plant Biology</topic><topic>Protein Conformation</topic><topic>Protein Kinases - chemistry</topic><topic>Protein Kinases - physiology</topic><topic>Proteins</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lemeille, Sylvain</creatorcontrib><creatorcontrib>Willig, Adrian</creatorcontrib><creatorcontrib>Depège-Fargeix, Nathalie</creatorcontrib><creatorcontrib>Delessert, Christian</creatorcontrib><creatorcontrib>Bassi, Roberto</creatorcontrib><creatorcontrib>Rochaix, Jean-David</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Environment Abstracts</collection><collection>Sustainability Science Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><collection>PLoS Biology</collection><jtitle>PLoS biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lemeille, Sylvain</au><au>Willig, Adrian</au><au>Depège-Fargeix, Nathalie</au><au>Delessert, Christian</au><au>Bassi, Roberto</au><au>Rochaix, Jean-David</au><au>Grossman, Arthur R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of the chloroplast protein kinase Stt7 during state transitions</atitle><jtitle>PLoS biology</jtitle><addtitle>PLoS Biol</addtitle><date>2009-03-01</date><risdate>2009</risdate><volume>7</volume><issue>3</issue><spage>e45</spage><epage>e1000045</epage><pages>e45-e1000045</pages><issn>1545-7885</issn><issn>1544-9173</issn><eissn>1545-7885</eissn><abstract>State transitions allow for the balancing of the light excitation energy between photosystem I and photosystem II and for optimal photosynthetic activity when photosynthetic organisms are subjected to changing light conditions. This process is regulated by the redox state of the plastoquinone pool through the Stt7/STN7 protein kinase required for phosphorylation of the light-harvesting complex LHCII and for the reversible displacement of the mobile LHCII between the photosystems. We show that Stt7 is associated with photosynthetic complexes including LHCII, photosystem I, and the cytochrome b6f complex. Our data reveal that Stt7 acts in catalytic amounts. We also provide evidence that Stt7 contains a transmembrane region that separates its catalytic kinase domain on the stromal side from its N-terminal end in the thylakoid lumen with two conserved Cys that are critical for its activity and state transitions. On the basis of these data, we propose that the activity of Stt7 is regulated through its transmembrane domain and that a disulfide bond between the two lumen Cys is essential for its activity. The high-light-induced reduction of this bond may occur through a transthylakoid thiol-reducing pathway driven by the ferredoxin-thioredoxin system which is also required for cytochrome b6f assembly and heme biogenesis.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>19260761</pmid><doi>10.1371/journal.pbio.1000045</doi><oa>free_for_read</oa></addata></record> |
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subjects | Adaptation, Physiological Algal Proteins - chemistry Algal Proteins - physiology Animals Bands Chlamydomonas - enzymology Chlamydomonas - physiology Chlorophyll Chloroplasts Chloroplasts - enzymology Chloroplasts - physiology Cytochrome b6f Complex - physiology Kinases Light Light-Harvesting Protein Complexes - physiology Phosphorylation Photosynthesis Photosynthesis - physiology Photosystem I Protein Complex - physiology Photosystem II Protein Complex - physiology Plant Biology Protein Conformation Protein Kinases - chemistry Protein Kinases - physiology Proteins Structure-Activity Relationship |
title | Analysis of the chloroplast protein kinase Stt7 during state transitions |
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