Purification properties and biogenesis of Chlamydomonas reinhardii photosystem I reaction center
A photosystem I reaction center was isolated from Chlamydomonas reinhardii chloroplasts. It consists of four different polypeptides with Mr approximately 70,000 (subunit I), 19,000 (subunit II), 10,000 (subunit III), and 8,000 (subunit IV). In the presence of salts, the purified reaction center was...
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| Veröffentlicht in: | The Journal of biological chemistry 1981-11, Vol.256 (22), p.11624-11628 |
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| creator | Nechushtai, R Nelson, N |
| description | A photosystem I reaction center was isolated from Chlamydomonas reinhardii chloroplasts. It consists of four different polypeptides
with Mr approximately 70,000 (subunit I), 19,000 (subunit II), 10,000 (subunit III), and 8,000 (subunit IV). In the presence
of salts, the purified reaction center was active in cytochrome 552 photooxidation. Short term labeling experiments with [35S]sulfate
revealed that subunit III contains no cysteine or methionine. Subunits I and IV were shown to be chloroplast translation products,
while subunit II appears to be synthesized on cytoplasmic ribosomes. The site of synthesis of the subunits to the proton-ATPase
complex was studied. A differential effect of cycloheximide on the assembly of photosystem I reaction center and the proton-ATPase
complex was indicated. |
| doi_str_mv | 10.1016/S0021-9258(19)68450-4 |
| format | Article |
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with Mr approximately 70,000 (subunit I), 19,000 (subunit II), 10,000 (subunit III), and 8,000 (subunit IV). In the presence
of salts, the purified reaction center was active in cytochrome 552 photooxidation. Short term labeling experiments with [35S]sulfate
revealed that subunit III contains no cysteine or methionine. Subunits I and IV were shown to be chloroplast translation products,
while subunit II appears to be synthesized on cytoplasmic ribosomes. The site of synthesis of the subunits to the proton-ATPase
complex was studied. A differential effect of cycloheximide on the assembly of photosystem I reaction center and the proton-ATPase
complex was indicated.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)68450-4</identifier><identifier>PMID: 7028739</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Algae ; Chlamydomonas - drug effects ; Chlamydomonas - metabolism ; Chlamydomonas reinhardtii ; Chloramphenicol - pharmacology ; chloroplasts ; Cycloheximide - pharmacology ; Molecular Weight ; Oxidation-Reduction ; Photosynthesis ; Photosynthetic Reaction Center Complex Proteins ; photosystem I ; Photosystem I Protein Complex ; Plant Proteins - isolation & purification ; Plant Proteins - metabolism ; proteins ; purification</subject><ispartof>The Journal of biological chemistry, 1981-11, Vol.256 (22), p.11624-11628</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c435t-6d81b8a2d7ce7ad9963e74e8c899d4f8c5044099d09ab7ca42e2459e5e17fa753</citedby><cites>FETCH-LOGICAL-c435t-6d81b8a2d7ce7ad9963e74e8c899d4f8c5044099d09ab7ca42e2459e5e17fa753</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7028739$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nechushtai, R</creatorcontrib><creatorcontrib>Nelson, N</creatorcontrib><title>Purification properties and biogenesis of Chlamydomonas reinhardii photosystem I reaction center</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A photosystem I reaction center was isolated from Chlamydomonas reinhardii chloroplasts. It consists of four different polypeptides
with Mr approximately 70,000 (subunit I), 19,000 (subunit II), 10,000 (subunit III), and 8,000 (subunit IV). In the presence
of salts, the purified reaction center was active in cytochrome 552 photooxidation. Short term labeling experiments with [35S]sulfate
revealed that subunit III contains no cysteine or methionine. Subunits I and IV were shown to be chloroplast translation products,
while subunit II appears to be synthesized on cytoplasmic ribosomes. The site of synthesis of the subunits to the proton-ATPase
complex was studied. A differential effect of cycloheximide on the assembly of photosystem I reaction center and the proton-ATPase
complex was indicated.</description><subject>Algae</subject><subject>Chlamydomonas - drug effects</subject><subject>Chlamydomonas - metabolism</subject><subject>Chlamydomonas reinhardtii</subject><subject>Chloramphenicol - pharmacology</subject><subject>chloroplasts</subject><subject>Cycloheximide - pharmacology</subject><subject>Molecular Weight</subject><subject>Oxidation-Reduction</subject><subject>Photosynthesis</subject><subject>Photosynthetic Reaction Center Complex Proteins</subject><subject>photosystem I</subject><subject>Photosystem I Protein Complex</subject><subject>Plant Proteins - isolation & purification</subject><subject>Plant Proteins - metabolism</subject><subject>proteins</subject><subject>purification</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtr3DAUhUVpSSZpf0KIF6UkC6e6emsZhuYBgRaSQHeqRr4eq4ytqeShzL-v50G21UaC891z0TmEXAC9AQrq6zOlDGrLpLkCe62MkLQW78gMqOE1l_DzPZm9IafkrJTfdDrCwgk50ZQZze2M_PqxybGNwY8xDdU6pzXmMWKp_NBUi5iWOGCJpUptNe9Wvt82qU-DL1XGOHQ-NzFW6y6NqWzLiH31OAk-7M0CDiPmj-RD61cFPx3vc_J69-1l_lA_fb9_nN8-1UFwOdaqMbAwnjU6oPaNtYqjFmiCsbYRrQmSCkGnN7V-oYMXDJmQFiWCbr2W_Jx8OfhOf_izwTK6PpaAq5UfMG2K01xZJSn9LwiSKyZhB8oDGHIqJWPr1jn2Pm8dULerwO0rcLt8HVi3r8CJae7iuGCz6LF5mzpmPumfD3oXl93fmNFNOYcOe8ekcow5AMV2NpcHrPXJ-WWOxb0-Mwp8spFSUsn_AXKMmE0</recordid><startdate>19811125</startdate><enddate>19811125</enddate><creator>Nechushtai, R</creator><creator>Nelson, N</creator><general>American Society for Biochemistry and Molecular Biology</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19811125</creationdate><title>Purification properties and biogenesis of Chlamydomonas reinhardii photosystem I reaction center</title><author>Nechushtai, R ; Nelson, N</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c435t-6d81b8a2d7ce7ad9963e74e8c899d4f8c5044099d09ab7ca42e2459e5e17fa753</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Algae</topic><topic>Chlamydomonas - drug effects</topic><topic>Chlamydomonas - metabolism</topic><topic>Chlamydomonas reinhardtii</topic><topic>Chloramphenicol - pharmacology</topic><topic>chloroplasts</topic><topic>Cycloheximide - pharmacology</topic><topic>Molecular Weight</topic><topic>Oxidation-Reduction</topic><topic>Photosynthesis</topic><topic>Photosynthetic Reaction Center Complex Proteins</topic><topic>photosystem I</topic><topic>Photosystem I Protein Complex</topic><topic>Plant Proteins - isolation & purification</topic><topic>Plant Proteins - metabolism</topic><topic>proteins</topic><topic>purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nechushtai, R</creatorcontrib><creatorcontrib>Nelson, N</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nechushtai, R</au><au>Nelson, N</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification properties and biogenesis of Chlamydomonas reinhardii photosystem I reaction center</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1981-11-25</date><risdate>1981</risdate><volume>256</volume><issue>22</issue><spage>11624</spage><epage>11628</epage><pages>11624-11628</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>A photosystem I reaction center was isolated from Chlamydomonas reinhardii chloroplasts. It consists of four different polypeptides
with Mr approximately 70,000 (subunit I), 19,000 (subunit II), 10,000 (subunit III), and 8,000 (subunit IV). In the presence
of salts, the purified reaction center was active in cytochrome 552 photooxidation. Short term labeling experiments with [35S]sulfate
revealed that subunit III contains no cysteine or methionine. Subunits I and IV were shown to be chloroplast translation products,
while subunit II appears to be synthesized on cytoplasmic ribosomes. The site of synthesis of the subunits to the proton-ATPase
complex was studied. A differential effect of cycloheximide on the assembly of photosystem I reaction center and the proton-ATPase
complex was indicated.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7028739</pmid><doi>10.1016/S0021-9258(19)68450-4</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1981-11, Vol.256 (22), p.11624-11628 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73696500 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Algae Chlamydomonas - drug effects Chlamydomonas - metabolism Chlamydomonas reinhardtii Chloramphenicol - pharmacology chloroplasts Cycloheximide - pharmacology Molecular Weight Oxidation-Reduction Photosynthesis Photosynthetic Reaction Center Complex Proteins photosystem I Photosystem I Protein Complex Plant Proteins - isolation & purification Plant Proteins - metabolism proteins purification |
| title | Purification properties and biogenesis of Chlamydomonas reinhardii photosystem I reaction center |
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