Phosphorylation of spinach chlorophyll-protein complexes CPII, but not CP29, CP27, or CP24, is phosphorylated in vitro
Previous studies have indicated that the reversible phosphorylation of a population of antenna complexes that can donate energy to PS II (‘mobile LHC II’) plays a regulatory role in the state 1—state 2 transition in thylakoid membranes. The relationship of phosphorylated LHC II to the multiple PS II...
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| Veröffentlicht in: | FEBS letters 1987-05, Vol.215 (1), p.25-30 |
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| creator | Dunahay, Terri G. Schuster, Gadi Staehelin, L.Andrew |
| description | Previous studies have indicated that the reversible phosphorylation of a population of antenna complexes that can donate energy to PS II (‘mobile LHC II’) plays a regulatory role in the state 1—state 2 transition in thylakoid membranes. The relationship of phosphorylated LHC II to the multiple PS II-associated chlorophyll a/b-proteins resolvable on green gels is currently unclear. We have used a high resolution gel system to analyze thylakoids phosphorylated in vitro. The only PS II-associated antenna complex to become phosphorylated is CPII*, indicating that this complex represents the mobile LHC II. The other putative PS II antenna complexes, CP29, CP24, and the new complex designated CP27 which comigrates with CPII, are not phosphorylated and are probably components of the bound ‘LHC II’ antenna. |
| doi_str_mv | 10.1016/0014-5793(87)80107-2 |
| format | Article |
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The relationship of phosphorylated LHC II to the multiple PS II-associated chlorophyll a/b-proteins resolvable on green gels is currently unclear. We have used a high resolution gel system to analyze thylakoids phosphorylated in vitro. The only PS II-associated antenna complex to become phosphorylated is CPII*, indicating that this complex represents the mobile LHC II. The other putative PS II antenna complexes, CP29, CP24, and the new complex designated CP27 which comigrates with CPII, are not phosphorylated and are probably components of the bound ‘LHC II’ antenna.</description><subject>Biological and medical sciences</subject><subject>Cell structures and functions</subject><subject>Chlorophyll - metabolism</subject><subject>Chlorophyll a/b-light harvesting complex</subject><subject>Chloroplast, photosynthetic membrane and photosynthesis</subject><subject>Chloroplasts - analysis</subject><subject>CP29</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>LHC II</subject><subject>Light-Harvesting Protein Complexes</subject><subject>Molecular and cellular biology</subject><subject>Phosphorylation</subject><subject>Photosynthetic Reaction Center Complex Proteins</subject><subject>Plant Proteins - metabolism</subject><subject>Plants - metabolism</subject><subject>Protein phosphorylation</subject><subject>Spinach</subject><subject>State 1—state 2 transition</subject><subject>Thylakoid</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE2P0zAQhi3EaikL_wAkHxACqQF_JU4uK0G1XSqtxB7gbDnOWDFy42Cnhf77dbZVxQntxfbMPPPO-EXoDSWfKKHVZ0KoKErZ8A-1_FgTSmTBnqEFrSUvuKjq52hxRl6glyn9IjmuaXOJLnlZMsnFAu3v-5DGPsSD15MLAw4Wp9EN2vTY9D7EMPYH74sxhgncgE3Yjh7-QsKr-81midvdhIcw5Yg1y_mUSxzi_BBL7BIe_5GHDmeFvZtieIUurPYJXp_uK_RzffNj9a24-367WX25K4yghBW0EszwBjhlZVXRTlrRge24rUHQrml52wJYISijQLkgmpXQtpU2uuQWGsqv0Pujbt7_9w7SpLYuGfBeDxB2SUkpalHSKoPiCJoYUopg1RjdVseDokTNdqvZSzV7qWqpHu1WLLe9Penv2i1056aTv7n-7lTXyWhvox6MS2dMlrxqWJOx9RH74zwcnjRarW--srkw52v5mJ33uT4KQTZ17yCqZBwMBjoXwUyqC-7_H3oAuIyuBA</recordid><startdate>19870504</startdate><enddate>19870504</enddate><creator>Dunahay, Terri G.</creator><creator>Schuster, Gadi</creator><creator>Staehelin, L.Andrew</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</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>7X8</scope></search><sort><creationdate>19870504</creationdate><title>Phosphorylation of spinach chlorophyll-protein complexes CPII, but not CP29, CP27, or CP24, is phosphorylated in vitro</title><author>Dunahay, Terri G. ; Schuster, Gadi ; Staehelin, L.Andrew</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4102-1642c39e3125661d7f4defd3f8e41d9b3bbeef44121e1340a25ebb6aca53fe913</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Biological and medical sciences</topic><topic>Cell structures and functions</topic><topic>Chlorophyll - metabolism</topic><topic>Chlorophyll a/b-light harvesting complex</topic><topic>Chloroplast, photosynthetic membrane and photosynthesis</topic><topic>Chloroplasts - analysis</topic><topic>CP29</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>LHC II</topic><topic>Light-Harvesting Protein Complexes</topic><topic>Molecular and cellular biology</topic><topic>Phosphorylation</topic><topic>Photosynthetic Reaction Center Complex Proteins</topic><topic>Plant Proteins - metabolism</topic><topic>Plants - metabolism</topic><topic>Protein phosphorylation</topic><topic>Spinach</topic><topic>State 1—state 2 transition</topic><topic>Thylakoid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dunahay, Terri G.</creatorcontrib><creatorcontrib>Schuster, Gadi</creatorcontrib><creatorcontrib>Staehelin, L.Andrew</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dunahay, Terri G.</au><au>Schuster, Gadi</au><au>Staehelin, L.Andrew</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation of spinach chlorophyll-protein complexes CPII, but not CP29, CP27, or CP24, is phosphorylated in vitro</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1987-05-04</date><risdate>1987</risdate><volume>215</volume><issue>1</issue><spage>25</spage><epage>30</epage><pages>25-30</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>Previous studies have indicated that the reversible phosphorylation of a population of antenna complexes that can donate energy to PS II (‘mobile LHC II’) plays a regulatory role in the state 1—state 2 transition in thylakoid membranes. The relationship of phosphorylated LHC II to the multiple PS II-associated chlorophyll a/b-proteins resolvable on green gels is currently unclear. We have used a high resolution gel system to analyze thylakoids phosphorylated in vitro. The only PS II-associated antenna complex to become phosphorylated is CPII*, indicating that this complex represents the mobile LHC II. The other putative PS II antenna complexes, CP29, CP24, and the new complex designated CP27 which comigrates with CPII, are not phosphorylated and are probably components of the bound ‘LHC II’ antenna.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>3552734</pmid><doi>10.1016/0014-5793(87)80107-2</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1987-05, Vol.215 (1), p.25-30 |
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| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection; Elsevier ScienceDirect Journals Collection; EZB Electronic Journals Library |
| subjects | Biological and medical sciences Cell structures and functions Chlorophyll - metabolism Chlorophyll a/b-light harvesting complex Chloroplast, photosynthetic membrane and photosynthesis Chloroplasts - analysis CP29 Fundamental and applied biological sciences. Psychology LHC II Light-Harvesting Protein Complexes Molecular and cellular biology Phosphorylation Photosynthetic Reaction Center Complex Proteins Plant Proteins - metabolism Plants - metabolism Protein phosphorylation Spinach State 1—state 2 transition Thylakoid |
| title | Phosphorylation of spinach chlorophyll-protein complexes CPII, but not CP29, CP27, or CP24, is phosphorylated in vitro |
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