Involvement of a Chloroplast HSP70 Heat Shock Protein in the Integration of a Protein (Light-Harvesting Complex Protien Precursor) into the Thylakoid Membrane
Molecular chaperones, including those belonging to the 70-kDa family of heat shock proteins (HSP70), assist both the translocation of proteins across membranes and their assembly into oligomeric complexes. We purified a chloroplast HSP70 (ct-HSP70) and demonstrated that it plays a major role in the...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1992-06, Vol.89 (12), p.5616-5619 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Yalovsky, Shaul Paulsen, Harald Michaeli, Dorit Chitnis, Parag R. Nechushtai, Rachel |
| description | Molecular chaperones, including those belonging to the 70-kDa family of heat shock proteins (HSP70), assist both the translocation of proteins across membranes and their assembly into oligomeric complexes. We purified a chloroplast HSP70 (ct-HSP70) and demonstrated that it plays a major role in the insertion of the precursor of the major light-harvesting complex of photosystem II (pLHCP; an integral membrane protein) into the thylakoids (the inner membranes of the chloroplast). Addition of the purified ct-HSP70 is necessary for efficient insertion of pLHCP into isolated thylakoid membranes. This activity of the purified ct-HSP70 is similar to that previously reported for the total stromal extract. When the chloroplast stromal extract is depleted of HSP70, a correlative reduction in the insertion activity of pLHCP is observed. The interaction between the ct-HSP70 and pLHCP involves physical association. The purified HSP70 acts directly on the membrane protein, presumably prevents its refolding, and thereby helps to maintain its competence for insertion into membranes. |
| doi_str_mv | 10.1073/pnas.89.12.5616 |
| format | Article |
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We purified a chloroplast HSP70 (ct-HSP70) and demonstrated that it plays a major role in the insertion of the precursor of the major light-harvesting complex of photosystem II (pLHCP; an integral membrane protein) into the thylakoids (the inner membranes of the chloroplast). Addition of the purified ct-HSP70 is necessary for efficient insertion of pLHCP into isolated thylakoid membranes. This activity of the purified ct-HSP70 is similar to that previously reported for the total stromal extract. When the chloroplast stromal extract is depleted of HSP70, a correlative reduction in the insertion activity of pLHCP is observed. The interaction between the ct-HSP70 and pLHCP involves physical association. The purified HSP70 acts directly on the membrane protein, presumably prevents its refolding, and thereby helps to maintain its competence for insertion into membranes.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.89.12.5616</identifier><identifier>PMID: 11607301</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Antibodies ; Biology ; Botany ; Chloroplasts ; Fluorescence ; Gels ; Heat shock proteins ; Hsp70 protein ; insertion ; light-harvesting complex ; photosystem II ; Physics ; Plants ; Polyclonal antibodies ; precursors ; Protein precursors ; Protein refolding ; Proteins ; role ; thylakoid membranes ; Thylakoids</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1992-06, Vol.89 (12), p.5616-5619</ispartof><rights>Copyright 1992 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Jun 15, 1992</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c521t-c292a6a1adf6fc743d07e764f26876b3e500a1171b83701a3e65543e19296dec3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/89/12.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2359704$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2359704$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27923,27924,53790,53792,58016,58249</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11607301$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yalovsky, Shaul</creatorcontrib><creatorcontrib>Paulsen, Harald</creatorcontrib><creatorcontrib>Michaeli, Dorit</creatorcontrib><creatorcontrib>Chitnis, Parag R.</creatorcontrib><creatorcontrib>Nechushtai, Rachel</creatorcontrib><title>Involvement of a Chloroplast HSP70 Heat Shock Protein in the Integration of a Protein (Light-Harvesting Complex Protien Precursor) into the Thylakoid Membrane</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Molecular chaperones, including those belonging to the 70-kDa family of heat shock proteins (HSP70), assist both the translocation of proteins across membranes and their assembly into oligomeric complexes. We purified a chloroplast HSP70 (ct-HSP70) and demonstrated that it plays a major role in the insertion of the precursor of the major light-harvesting complex of photosystem II (pLHCP; an integral membrane protein) into the thylakoids (the inner membranes of the chloroplast). Addition of the purified ct-HSP70 is necessary for efficient insertion of pLHCP into isolated thylakoid membranes. This activity of the purified ct-HSP70 is similar to that previously reported for the total stromal extract. When the chloroplast stromal extract is depleted of HSP70, a correlative reduction in the insertion activity of pLHCP is observed. The interaction between the ct-HSP70 and pLHCP involves physical association. The purified HSP70 acts directly on the membrane protein, presumably prevents its refolding, and thereby helps to maintain its competence for insertion into membranes.</description><subject>Antibodies</subject><subject>Biology</subject><subject>Botany</subject><subject>Chloroplasts</subject><subject>Fluorescence</subject><subject>Gels</subject><subject>Heat shock proteins</subject><subject>Hsp70 protein</subject><subject>insertion</subject><subject>light-harvesting complex</subject><subject>photosystem II</subject><subject>Physics</subject><subject>Plants</subject><subject>Polyclonal antibodies</subject><subject>precursors</subject><subject>Protein precursors</subject><subject>Protein refolding</subject><subject>Proteins</subject><subject>role</subject><subject>thylakoid membranes</subject><subject>Thylakoids</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><recordid>eNqFkl-LEzEUxQdR3O7qsy8iwYdVH6abm8wkE_BFitpCxYVdn0M6zXSmm0lqkim7X8bParrt_lEEIXAf7u8cci4ny14BHgPm9GxjVRhXYgxkXDJgT7IRYAE5KwR-mo0wJjyvClIcZcchrDHGoqzw8-wIgCU1hlH2a2a3zmx1r21ErkEKTVrjvNsYFSKaXpxzjKZaRXTRuvoKnXsXdWdRerHVaGajXnkVO2f34rv9-3m3amM-VX6rQ-zsCk1cvzH6-pbotE1T14MPzn9IZtHd2l22N0ZduW6Jvul-4ZXVL7JnjTJBvzzMk-zHl8-Xk2k-__51Nvk0z-uSQMxrIohiCtSyYU3NC7rEXHNWNIRVnC2oLjFWABwWFeUYFNWsLAuqQRDBlrqmJ9nHve9mWPR6WadreGXkxne98jfSqU7-ubFdK1duKwtBC5rkpwe5dz-HlFj2Xai1MSmCG4LkhENFCv5fEBgBSilO4Nu_wLUbvE03kAQD4SUVO7ezPVR7F4LXzf2HActdP-SuH7ISEojc9SMp3jzO-cAfCpGAdwdgp7xbPzjIZjAm6uv4yOrfZAJe74F1iM7fE4SWguOC_gYGutmb</recordid><startdate>19920615</startdate><enddate>19920615</enddate><creator>Yalovsky, Shaul</creator><creator>Paulsen, Harald</creator><creator>Michaeli, Dorit</creator><creator>Chitnis, Parag R.</creator><creator>Nechushtai, Rachel</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><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>M7Z</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19920615</creationdate><title>Involvement of a Chloroplast HSP70 Heat Shock Protein in the Integration of a Protein (Light-Harvesting Complex Protien Precursor) into the Thylakoid Membrane</title><author>Yalovsky, Shaul ; Paulsen, Harald ; Michaeli, Dorit ; Chitnis, Parag R. ; Nechushtai, Rachel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c521t-c292a6a1adf6fc743d07e764f26876b3e500a1171b83701a3e65543e19296dec3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Antibodies</topic><topic>Biology</topic><topic>Botany</topic><topic>Chloroplasts</topic><topic>Fluorescence</topic><topic>Gels</topic><topic>Heat shock proteins</topic><topic>Hsp70 protein</topic><topic>insertion</topic><topic>light-harvesting complex</topic><topic>photosystem II</topic><topic>Physics</topic><topic>Plants</topic><topic>Polyclonal antibodies</topic><topic>precursors</topic><topic>Protein precursors</topic><topic>Protein refolding</topic><topic>Proteins</topic><topic>role</topic><topic>thylakoid membranes</topic><topic>Thylakoids</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yalovsky, Shaul</creatorcontrib><creatorcontrib>Paulsen, Harald</creatorcontrib><creatorcontrib>Michaeli, Dorit</creatorcontrib><creatorcontrib>Chitnis, Parag R.</creatorcontrib><creatorcontrib>Nechushtai, Rachel</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Biochemistry Abstracts 1</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yalovsky, Shaul</au><au>Paulsen, Harald</au><au>Michaeli, Dorit</au><au>Chitnis, Parag R.</au><au>Nechushtai, Rachel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Involvement of a Chloroplast HSP70 Heat Shock Protein in the Integration of a Protein (Light-Harvesting Complex Protien Precursor) into the Thylakoid Membrane</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1992-06-15</date><risdate>1992</risdate><volume>89</volume><issue>12</issue><spage>5616</spage><epage>5619</epage><pages>5616-5619</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Molecular chaperones, including those belonging to the 70-kDa family of heat shock proteins (HSP70), assist both the translocation of proteins across membranes and their assembly into oligomeric complexes. We purified a chloroplast HSP70 (ct-HSP70) and demonstrated that it plays a major role in the insertion of the precursor of the major light-harvesting complex of photosystem II (pLHCP; an integral membrane protein) into the thylakoids (the inner membranes of the chloroplast). Addition of the purified ct-HSP70 is necessary for efficient insertion of pLHCP into isolated thylakoid membranes. This activity of the purified ct-HSP70 is similar to that previously reported for the total stromal extract. When the chloroplast stromal extract is depleted of HSP70, a correlative reduction in the insertion activity of pLHCP is observed. The interaction between the ct-HSP70 and pLHCP involves physical association. The purified HSP70 acts directly on the membrane protein, presumably prevents its refolding, and thereby helps to maintain its competence for insertion into membranes.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>11607301</pmid><doi>10.1073/pnas.89.12.5616</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1992-06, Vol.89 (12), p.5616-5619 |
| issn | 0027-8424 1091-6490 |
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| source | JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Antibodies Biology Botany Chloroplasts Fluorescence Gels Heat shock proteins Hsp70 protein insertion light-harvesting complex photosystem II Physics Plants Polyclonal antibodies precursors Protein precursors Protein refolding Proteins role thylakoid membranes Thylakoids |
| title | Involvement of a Chloroplast HSP70 Heat Shock Protein in the Integration of a Protein (Light-Harvesting Complex Protien Precursor) into the Thylakoid Membrane |
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