Physiologically active chloroplasts contain pools of unassembled extrinsic proteins of the photosynthetic oxygen-evolving enzyme complex in the thylakoid lumen
The oxygen-evolving complex (OEC) of photosystem II (PS II) consists of at least three extrinsic membrane-associated protein subunits, OE33, OE23, and OE17, with associated Mn2+,Ca2+, and Cl- ions. These subunits are bound to the lumen side of PS II core proteins embedded in the thylakoid membrane....
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| Veröffentlicht in: | The Journal of cell biology 1991-10, Vol.115 (2), p.321-328 |
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| creator | Ettinger, W.F. (University of California, Davis, CA) Theg, S.M |
| description | The oxygen-evolving complex (OEC) of photosystem II (PS II) consists of at least three extrinsic membrane-associated protein subunits, OE33, OE23, and OE17, with associated Mn2+,Ca2+, and Cl- ions. These subunits are bound to the lumen side of PS II core proteins embedded in the thylakoid membrane. Our experiments reveal that a significant fraction of each subunit is normally present in unassembled pools within the thylakoid lumen. This conclusion was supported by immunological detection of free subunits after freshly isolated pea thylakoids were fractionated with low levels of Triton X-100. Plastocyanin, a soluble lumen protein, was completely released from the lumen by 0.04% Triton X-100. This gentle detergent treatment also caused the release from the thylakoids of between 10 and 20%, 40 and 60%, and 15 and 50% of OE33, OE23, and OE17, respectively. Measurements of the rates of oxygen evolution from Triton-treated thylakoids, both in the presence and absence of Ca2+, and before and after incubation with hydroquinone, demonstrated that the OEC was not dissociated by the detergent treatment. Thylakoids isolated from spinach released similar amounts of extrinsic proteins after Triton treatment. These data demonstrate that physiologically active chloroplasts contain significant pools of unassembled extrinsic OEC polypeptide subunits free in the lumen of the thylakoids. |
| doi_str_mv | 10.1083/jcb.115.2.321 |
| format | Article |
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(University of California, Davis, CA) ; Theg, S.M</creator><creatorcontrib>Ettinger, W.F. (University of California, Davis, CA) ; Theg, S.M</creatorcontrib><description>The oxygen-evolving complex (OEC) of photosystem II (PS II) consists of at least three extrinsic membrane-associated protein subunits, OE33, OE23, and OE17, with associated Mn2+,Ca2+, and Cl- ions. These subunits are bound to the lumen side of PS II core proteins embedded in the thylakoid membrane. Our experiments reveal that a significant fraction of each subunit is normally present in unassembled pools within the thylakoid lumen. This conclusion was supported by immunological detection of free subunits after freshly isolated pea thylakoids were fractionated with low levels of Triton X-100. Plastocyanin, a soluble lumen protein, was completely released from the lumen by 0.04% Triton X-100. This gentle detergent treatment also caused the release from the thylakoids of between 10 and 20%, 40 and 60%, and 15 and 50% of OE33, OE23, and OE17, respectively. Measurements of the rates of oxygen evolution from Triton-treated thylakoids, both in the presence and absence of Ca2+, and before and after incubation with hydroquinone, demonstrated that the OEC was not dissociated by the detergent treatment. Thylakoids isolated from spinach released similar amounts of extrinsic proteins after Triton treatment. These data demonstrate that physiologically active chloroplasts contain significant pools of unassembled extrinsic OEC polypeptide subunits free in the lumen of the thylakoids.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.115.2.321</identifier><identifier>PMID: 1918144</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>New York, NY: Rockefeller University Press</publisher><subject>Biological and medical sciences ; Calcium - pharmacology ; Cell biochemistry ; Cell Fractionation ; Cell physiology ; Chlorophylls ; CHLOROPLASTE ; CHLOROPLASTS ; Chloroplasts - chemistry ; Chloroplasts - drug effects ; Chloroplasts - metabolism ; CLOROPLASTO ; Detergents ; Electrophoresis, Polyacrylamide Gel ; Fabaceae ; FOTOSINTESIS ; Fundamental and applied biological sciences. Psychology ; Hydroquinones ; Hydroquinones - pharmacology ; Macromolecular Substances ; Membrane Proteins - metabolism ; Octoxynol ; Oxygen ; Oxygen - metabolism ; Oxygen evolving complex ; Peas ; PHOTOSYNTHESE ; PHOTOSYNTHESIS ; Photosynthetic Reaction Center Complex Proteins - metabolism ; PHOTOSYSTEM II ; Photosystem II Protein Complex ; Plant physiology and development ; Plant Proteins - metabolism ; Plants, Medicinal ; PLASTE ; PLASTIDIOS ; PLASTIDS ; Polyethylene Glycols - pharmacology ; PROTEINAS ; PROTEINE ; PROTEINS ; Spinach ; Spinacia oleracea ; Thylakoids</subject><ispartof>The Journal of cell biology, 1991-10, Vol.115 (2), p.321-328</ispartof><rights>Copyright 1991 The Rockefeller University Press</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c482t-a90aa0b244c268d09c5170719535e6639e527c778818c748b54a6577719d46bb3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,778,782,883,27907,27908</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4341024$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1918144$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ettinger, W.F. (University of California, Davis, CA)</creatorcontrib><creatorcontrib>Theg, S.M</creatorcontrib><title>Physiologically active chloroplasts contain pools of unassembled extrinsic proteins of the photosynthetic oxygen-evolving enzyme complex in the thylakoid lumen</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>The oxygen-evolving complex (OEC) of photosystem II (PS II) consists of at least three extrinsic membrane-associated protein subunits, OE33, OE23, and OE17, with associated Mn2+,Ca2+, and Cl- ions. These subunits are bound to the lumen side of PS II core proteins embedded in the thylakoid membrane. Our experiments reveal that a significant fraction of each subunit is normally present in unassembled pools within the thylakoid lumen. This conclusion was supported by immunological detection of free subunits after freshly isolated pea thylakoids were fractionated with low levels of Triton X-100. Plastocyanin, a soluble lumen protein, was completely released from the lumen by 0.04% Triton X-100. This gentle detergent treatment also caused the release from the thylakoids of between 10 and 20%, 40 and 60%, and 15 and 50% of OE33, OE23, and OE17, respectively. Measurements of the rates of oxygen evolution from Triton-treated thylakoids, both in the presence and absence of Ca2+, and before and after incubation with hydroquinone, demonstrated that the OEC was not dissociated by the detergent treatment. Thylakoids isolated from spinach released similar amounts of extrinsic proteins after Triton treatment. These data demonstrate that physiologically active chloroplasts contain significant pools of unassembled extrinsic OEC polypeptide subunits free in the lumen of the thylakoids.</description><subject>Biological and medical sciences</subject><subject>Calcium - pharmacology</subject><subject>Cell biochemistry</subject><subject>Cell Fractionation</subject><subject>Cell physiology</subject><subject>Chlorophylls</subject><subject>CHLOROPLASTE</subject><subject>CHLOROPLASTS</subject><subject>Chloroplasts - chemistry</subject><subject>Chloroplasts - drug effects</subject><subject>Chloroplasts - metabolism</subject><subject>CLOROPLASTO</subject><subject>Detergents</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fabaceae</subject><subject>FOTOSINTESIS</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydroquinones</subject><subject>Hydroquinones - pharmacology</subject><subject>Macromolecular Substances</subject><subject>Membrane Proteins - metabolism</subject><subject>Octoxynol</subject><subject>Oxygen</subject><subject>Oxygen - metabolism</subject><subject>Oxygen evolving complex</subject><subject>Peas</subject><subject>PHOTOSYNTHESE</subject><subject>PHOTOSYNTHESIS</subject><subject>Photosynthetic Reaction Center Complex Proteins - metabolism</subject><subject>PHOTOSYSTEM II</subject><subject>Photosystem II Protein Complex</subject><subject>Plant physiology and development</subject><subject>Plant Proteins - metabolism</subject><subject>Plants, Medicinal</subject><subject>PLASTE</subject><subject>PLASTIDIOS</subject><subject>PLASTIDS</subject><subject>Polyethylene Glycols - pharmacology</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PROTEINS</subject><subject>Spinach</subject><subject>Spinacia oleracea</subject><subject>Thylakoids</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkVGL1DAUhYso6-zqoy-ikAfxrWOSJm36IsjiqrCgoPsc0kxmmjHNrUk6TP0z_lVTZtjVp1w4X865l1MULwheEyyqd3vdrQnha7quKHlUrAhnuBSE4cfFCmNKypZT_rS4jHGPMWYNqy6KC9KSjLBV8edbP0cLDnZWK-dmpHSyB4N07yDA6FRMEWnwSVmPRgAXEWzR5FWMZuic2SBzTMH6aDUaAySTx4VIvUFjDwni7POcsgzHeWd8aQ7gDtbvkPG_5yEnwTA6c0TZf_mU-tmpn2A3yE2D8c-KJ1vlonl-fq-Ku5uPP64_l7dfP325_nBbaiZoKlWLlcIdZUzTWmxwqzlpcENaXnFT11VrOG100whBhG6Y6DhTNW-aTGxY3XXVVfH-5DtO3WA22vgUlJNjsIMKswRl5f-Kt73cwUFSKlrC6mzw9mwQ4NdkYpKDjdo4p7yBKUpSE8FrjDNYnkAdIMZgtvchBMulUZkblblRSWVuNPOv_93sgT5VmPU3Z13FXOE2KK9tvMdYxQimC_bqhO1jgvDgUuflxZLy8iRvFUi1C9nh7vtyGG6q6i_qdMAc</recordid><startdate>19911001</startdate><enddate>19911001</enddate><creator>Ettinger, W.F. (University of California, Davis, CA)</creator><creator>Theg, S.M</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><scope>FBQ</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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>5PM</scope></search><sort><creationdate>19911001</creationdate><title>Physiologically active chloroplasts contain pools of unassembled extrinsic proteins of the photosynthetic oxygen-evolving enzyme complex in the thylakoid lumen</title><author>Ettinger, W.F. (University of California, Davis, CA) ; Theg, S.M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c482t-a90aa0b244c268d09c5170719535e6639e527c778818c748b54a6577719d46bb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Biological and medical sciences</topic><topic>Calcium - pharmacology</topic><topic>Cell biochemistry</topic><topic>Cell Fractionation</topic><topic>Cell physiology</topic><topic>Chlorophylls</topic><topic>CHLOROPLASTE</topic><topic>CHLOROPLASTS</topic><topic>Chloroplasts - chemistry</topic><topic>Chloroplasts - drug effects</topic><topic>Chloroplasts - metabolism</topic><topic>CLOROPLASTO</topic><topic>Detergents</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fabaceae</topic><topic>FOTOSINTESIS</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydroquinones</topic><topic>Hydroquinones - pharmacology</topic><topic>Macromolecular Substances</topic><topic>Membrane Proteins - metabolism</topic><topic>Octoxynol</topic><topic>Oxygen</topic><topic>Oxygen - metabolism</topic><topic>Oxygen evolving complex</topic><topic>Peas</topic><topic>PHOTOSYNTHESE</topic><topic>PHOTOSYNTHESIS</topic><topic>Photosynthetic Reaction Center Complex Proteins - metabolism</topic><topic>PHOTOSYSTEM II</topic><topic>Photosystem II Protein Complex</topic><topic>Plant physiology and development</topic><topic>Plant Proteins - metabolism</topic><topic>Plants, Medicinal</topic><topic>PLASTE</topic><topic>PLASTIDIOS</topic><topic>PLASTIDS</topic><topic>Polyethylene Glycols - pharmacology</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEINS</topic><topic>Spinach</topic><topic>Spinacia oleracea</topic><topic>Thylakoids</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ettinger, W.F. (University of California, Davis, CA)</creatorcontrib><creatorcontrib>Theg, S.M</creatorcontrib><collection>AGRIS</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ettinger, W.F. (University of California, Davis, CA)</au><au>Theg, S.M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Physiologically active chloroplasts contain pools of unassembled extrinsic proteins of the photosynthetic oxygen-evolving enzyme complex in the thylakoid lumen</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1991-10-01</date><risdate>1991</risdate><volume>115</volume><issue>2</issue><spage>321</spage><epage>328</epage><pages>321-328</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>The oxygen-evolving complex (OEC) of photosystem II (PS II) consists of at least three extrinsic membrane-associated protein subunits, OE33, OE23, and OE17, with associated Mn2+,Ca2+, and Cl- ions. These subunits are bound to the lumen side of PS II core proteins embedded in the thylakoid membrane. Our experiments reveal that a significant fraction of each subunit is normally present in unassembled pools within the thylakoid lumen. This conclusion was supported by immunological detection of free subunits after freshly isolated pea thylakoids were fractionated with low levels of Triton X-100. Plastocyanin, a soluble lumen protein, was completely released from the lumen by 0.04% Triton X-100. This gentle detergent treatment also caused the release from the thylakoids of between 10 and 20%, 40 and 60%, and 15 and 50% of OE33, OE23, and OE17, respectively. Measurements of the rates of oxygen evolution from Triton-treated thylakoids, both in the presence and absence of Ca2+, and before and after incubation with hydroquinone, demonstrated that the OEC was not dissociated by the detergent treatment. Thylakoids isolated from spinach released similar amounts of extrinsic proteins after Triton treatment. These data demonstrate that physiologically active chloroplasts contain significant pools of unassembled extrinsic OEC polypeptide subunits free in the lumen of the thylakoids.</abstract><cop>New York, NY</cop><pub>Rockefeller University Press</pub><pmid>1918144</pmid><doi>10.1083/jcb.115.2.321</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of cell biology, 1991-10, Vol.115 (2), p.321-328 |
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| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Biological and medical sciences Calcium - pharmacology Cell biochemistry Cell Fractionation Cell physiology Chlorophylls CHLOROPLASTE CHLOROPLASTS Chloroplasts - chemistry Chloroplasts - drug effects Chloroplasts - metabolism CLOROPLASTO Detergents Electrophoresis, Polyacrylamide Gel Fabaceae FOTOSINTESIS Fundamental and applied biological sciences. Psychology Hydroquinones Hydroquinones - pharmacology Macromolecular Substances Membrane Proteins - metabolism Octoxynol Oxygen Oxygen - metabolism Oxygen evolving complex Peas PHOTOSYNTHESE PHOTOSYNTHESIS Photosynthetic Reaction Center Complex Proteins - metabolism PHOTOSYSTEM II Photosystem II Protein Complex Plant physiology and development Plant Proteins - metabolism Plants, Medicinal PLASTE PLASTIDIOS PLASTIDS Polyethylene Glycols - pharmacology PROTEINAS PROTEINE PROTEINS Spinach Spinacia oleracea Thylakoids |
| title | Physiologically active chloroplasts contain pools of unassembled extrinsic proteins of the photosynthetic oxygen-evolving enzyme complex in the thylakoid lumen |
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