Molecular chaperones are present in the thylakoid lumen of pea chloroplasts
A soluble protein fraction was obtained from pea chloroplast thylakoids, which represents highly enriched lumenal components. Using antisera against chaperonin 60 (cpn60), chaperonin 10 (cpn10) and the heat shock cognate protein of 70 kDa (hsc70) we are able to demonstrate, that the thylakoid lumen...
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| Veröffentlicht in: | FEBS letters 1996-02, Vol.379 (3), p.302-304 |
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| creator | Schlicher, Thomas Soll, Jürgen |
| description | A soluble protein fraction was obtained from pea chloroplast thylakoids, which represents highly enriched lumenal components. Using antisera against chaperonin 60 (cpn60), chaperonin 10 (cpn10) and the heat shock cognate protein of 70 kDa (hsc70) we are able to demonstrate, that the thylakoid lumen contains a separate set of molecular chaperones, which is distinct from the stromal one. In contrast to the α and β subunits of cpn60 present in the stroma the lumen contains only one cpn60 isoform of distinct isoelectric point. Furthermore the lumenal cpn10 is of ‘normal’ size and not like its stromal counterpart of a double-domain tandem architecture. The immunoreactive hsc70 isoforms in the lumen seem also to be different from the stromal ones. Thus, chloroplasts seem to contain the largest number of molecular chaperone isoforms present in one organelle. |
| doi_str_mv | 10.1016/0014-5793(95)01534-5 |
| format | Article |
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Using antisera against chaperonin 60 (cpn60), chaperonin 10 (cpn10) and the heat shock cognate protein of 70 kDa (hsc70) we are able to demonstrate, that the thylakoid lumen contains a separate set of molecular chaperones, which is distinct from the stromal one. In contrast to the α and β subunits of cpn60 present in the stroma the lumen contains only one cpn60 isoform of distinct isoelectric point. Furthermore the lumenal cpn10 is of ‘normal’ size and not like its stromal counterpart of a double-domain tandem architecture. The immunoreactive hsc70 isoforms in the lumen seem also to be different from the stromal ones. 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Using antisera against chaperonin 60 (cpn60), chaperonin 10 (cpn10) and the heat shock cognate protein of 70 kDa (hsc70) we are able to demonstrate, that the thylakoid lumen contains a separate set of molecular chaperones, which is distinct from the stromal one. In contrast to the α and β subunits of cpn60 present in the stroma the lumen contains only one cpn60 isoform of distinct isoelectric point. Furthermore the lumenal cpn10 is of ‘normal’ size and not like its stromal counterpart of a double-domain tandem architecture. The immunoreactive hsc70 isoforms in the lumen seem also to be different from the stromal ones. Thus, chloroplasts seem to contain the largest number of molecular chaperone isoforms present in one organelle.</description><subject>Chaperone</subject><subject>chaperonin</subject><subject>Chaperonin 10 - isolation & purification</subject><subject>Chaperonin 60 - isolation & purification</subject><subject>Chloroplasts - chemistry</subject><subject>cpn</subject><subject>heat shock cognate protein</subject><subject>hsc</subject><subject>HSP70 Heat-Shock Proteins - isolation & purification</subject><subject>Molecular Chaperones - isolation & purification</subject><subject>OEE</subject><subject>OEE of 33 kD</subject><subject>OEE33</subject><subject>oxygen evolving enzyme complex</subject><subject>Pisum sativum</subject><subject>Pisum sativum - chemistry</subject><subject>Pisum sativum L</subject><subject>Plant Proteins - isolation & purification</subject><subject>Protein assembly</subject><subject>ribulose-1,5-bis-phosphate carboxylase oxygenase</subject><subject>Rubisco</subject><subject>small subunit of Rubisco</subject><subject>SSU</subject><subject>Str</subject><subject>stroma fraction</subject><subject>Thylakoid lumen</subject><subject>thylakoid lumen fraction</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkFFv2yAUhVHVKU27_YNO8lPVPXgF2xh4mdRGSTc1VV-2Z4TxRWElxgV7Vf79cBL1sZsQQvfec85FH0KXBH8lmNQ3GJMqp0yU14J-wYSWqTpBc8JZmZdVzU_R_E1yhs5j_I1TzYmYoRmvcckImaOHR-9Aj06FTG9UD8F3EDMVIOsDROiGzHbZsIF0d049e9tmbtxCl3mT9aCSyfnge6fiED-iD0a5CJ-O7wX6tVr-XHzP10_3Pxa361xXgtFcNNSQluNW07YSGHjBuVEgFG4IU9wUjCpBmqYowDSk0KbFTJWswpAOrk15ga4OuX3wLyPEQW5t1OCc6sCPUTKW1rCK_FNIaI2ruhBJWB2EOvgYAxjZB7tVYScJlhNsOZGUE0kpqNzDljTZPh_zx2YL7ZvpSDfNV4f5q3Ww-69MuVreFdNg6gu6706Lvh2CIGH9YyHIqC10GlobQA-y9fb9n_4F-mGhXg</recordid><startdate>19960205</startdate><enddate>19960205</enddate><creator>Schlicher, Thomas</creator><creator>Soll, Jürgen</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7TM</scope><scope>7X8</scope></search><sort><creationdate>19960205</creationdate><title>Molecular chaperones are present in the thylakoid lumen of pea chloroplasts</title><author>Schlicher, Thomas ; Soll, Jürgen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4975-9b5f1d80dc5d490e8288fae9a0b17a8f275a91bb22efb12cfd07a3740e0e006f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Chaperone</topic><topic>chaperonin</topic><topic>Chaperonin 10 - isolation & purification</topic><topic>Chaperonin 60 - isolation & purification</topic><topic>Chloroplasts - chemistry</topic><topic>cpn</topic><topic>heat shock cognate protein</topic><topic>hsc</topic><topic>HSP70 Heat-Shock Proteins - isolation & purification</topic><topic>Molecular Chaperones - isolation & purification</topic><topic>OEE</topic><topic>OEE of 33 kD</topic><topic>OEE33</topic><topic>oxygen evolving enzyme complex</topic><topic>Pisum sativum</topic><topic>Pisum sativum - chemistry</topic><topic>Pisum sativum L</topic><topic>Plant Proteins - isolation & purification</topic><topic>Protein assembly</topic><topic>ribulose-1,5-bis-phosphate carboxylase oxygenase</topic><topic>Rubisco</topic><topic>small subunit of Rubisco</topic><topic>SSU</topic><topic>Str</topic><topic>stroma fraction</topic><topic>Thylakoid lumen</topic><topic>thylakoid lumen fraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schlicher, Thomas</creatorcontrib><creatorcontrib>Soll, Jürgen</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schlicher, Thomas</au><au>Soll, Jürgen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular chaperones are present in the thylakoid lumen of pea chloroplasts</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1996-02-05</date><risdate>1996</risdate><volume>379</volume><issue>3</issue><spage>302</spage><epage>304</epage><pages>302-304</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>A soluble protein fraction was obtained from pea chloroplast thylakoids, which represents highly enriched lumenal components. Using antisera against chaperonin 60 (cpn60), chaperonin 10 (cpn10) and the heat shock cognate protein of 70 kDa (hsc70) we are able to demonstrate, that the thylakoid lumen contains a separate set of molecular chaperones, which is distinct from the stromal one. In contrast to the α and β subunits of cpn60 present in the stroma the lumen contains only one cpn60 isoform of distinct isoelectric point. Furthermore the lumenal cpn10 is of ‘normal’ size and not like its stromal counterpart of a double-domain tandem architecture. The immunoreactive hsc70 isoforms in the lumen seem also to be different from the stromal ones. Thus, chloroplasts seem to contain the largest number of molecular chaperone isoforms present in one organelle.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>8603711</pmid><doi>10.1016/0014-5793(95)01534-5</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1996-02, Vol.379 (3), p.302-304 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77975741 |
| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Chaperone chaperonin Chaperonin 10 - isolation & purification Chaperonin 60 - isolation & purification Chloroplasts - chemistry cpn heat shock cognate protein hsc HSP70 Heat-Shock Proteins - isolation & purification Molecular Chaperones - isolation & purification OEE OEE of 33 kD OEE33 oxygen evolving enzyme complex Pisum sativum Pisum sativum - chemistry Pisum sativum L Plant Proteins - isolation & purification Protein assembly ribulose-1,5-bis-phosphate carboxylase oxygenase Rubisco small subunit of Rubisco SSU Str stroma fraction Thylakoid lumen thylakoid lumen fraction |
| title | Molecular chaperones are present in the thylakoid lumen of pea chloroplasts |
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