Chloroplast biogenesis: The use of mutants to study the etioplast-chloroplast transition
In angiosperm plants, the etioplast-chloroplast transition is light-dependent. A key factor in this process is the protochlorophyllide oxidoreductase A (PORA), which catalyzes the light-induced reduction of protochlorophyllide to chlorophyllide. The import pathway of the precursor protein prePORA in...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2007-01, Vol.104 (2), p.678-683 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Philippar, Katrin Geis, Tina Ilkavets, Iryna Oster, Ulrike Schwenkert, Serena Meurer, Jörg Soll, Jürgen |
| description | In angiosperm plants, the etioplast-chloroplast transition is light-dependent. A key factor in this process is the protochlorophyllide oxidoreductase A (PORA), which catalyzes the light-induced reduction of protochlorophyllide to chlorophyllide. The import pathway of the precursor protein prePORA into chloroplasts was analyzed in vivo and in vitro by using homozygous loss-of-function mutants in genes coding for chlorophyllide a oxygenase (CAO) or for members of the outer-envelope solute-channel protein family of 16 kDa (OEP16), both of which have been implied to be key factors for the import of prePORA. Our in vivo analyses show that cao or oep16 mutants contain a normally structured prolamellar body that contains the protochlorophyllide holochrome. Furthermore, etioplasts from cao and oep16 mutants contain PORA protein as found by mass spectrometry. Our data demonstrate that both CAO and OEP16 are dispensable for chloroplast biogenesis and play no central role in the import of prePORA in vivo and in vitro as further indicated by protein import studies. |
| doi_str_mv | 10.1073/pnas.0610062104 |
| format | Article |
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A key factor in this process is the protochlorophyllide oxidoreductase A (PORA), which catalyzes the light-induced reduction of protochlorophyllide to chlorophyllide. The import pathway of the precursor protein prePORA into chloroplasts was analyzed in vivo and in vitro by using homozygous loss-of-function mutants in genes coding for chlorophyllide a oxygenase (CAO) or for members of the outer-envelope solute-channel protein family of 16 kDa (OEP16), both of which have been implied to be key factors for the import of prePORA. Our in vivo analyses show that cao or oep16 mutants contain a normally structured prolamellar body that contains the protochlorophyllide holochrome. Furthermore, etioplasts from cao and oep16 mutants contain PORA protein as found by mass spectrometry. Our data demonstrate that both CAO and OEP16 are dispensable for chloroplast biogenesis and play no central role in the import of prePORA in vivo and in vitro as further indicated by protein import studies.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0610062104</identifier><identifier>PMID: 17202255</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Arabidopsis - genetics ; Arabidopsis - metabolism ; Arabidopsis - radiation effects ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Arabidopsis thaliana ; Base Sequence ; Biological Sciences ; Chlorophyll ; chlorophyllide a oxygenase ; Chlorophyllides - metabolism ; chloroplast biogenesis ; Chloroplasts ; Chloroplasts - genetics ; Chloroplasts - metabolism ; Chloroplasts - radiation effects ; Cotyledons ; cytochemistry ; DNA Primers - genetics ; Etioplasts ; Genes ; Genes, Plant ; Imports ; Ion Channels - genetics ; Ion Channels - metabolism ; mutants ; Mutation ; oxidoreductases ; oxygenases ; Oxygenases - genetics ; Oxygenases - metabolism ; phenotype ; Photobiology ; Plants ; Plastids ; Protein isoforms ; Protein precursors ; Protein Transport ; Proteins ; Protochlorophyllide - metabolism ; protochlorophyllide oxidoreductase A ; Seedlings</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2007-01, Vol.104 (2), p.678-683</ispartof><rights>Copyright 2007 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Jan 9, 2007</rights><rights>2007 by The National Academy of Sciences of the USA 2007</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c614t-413dd8f5ac7e88e922727e2c5dcb221258b0c01e9e37760d75441fc0639e77743</citedby><cites>FETCH-LOGICAL-c614t-413dd8f5ac7e88e922727e2c5dcb221258b0c01e9e37760d75441fc0639e77743</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/104/2.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/25426161$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/25426161$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,725,778,782,801,883,27907,27908,53774,53776,58000,58233</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17202255$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Philippar, Katrin</creatorcontrib><creatorcontrib>Geis, Tina</creatorcontrib><creatorcontrib>Ilkavets, Iryna</creatorcontrib><creatorcontrib>Oster, Ulrike</creatorcontrib><creatorcontrib>Schwenkert, Serena</creatorcontrib><creatorcontrib>Meurer, Jörg</creatorcontrib><creatorcontrib>Soll, Jürgen</creatorcontrib><title>Chloroplast biogenesis: The use of mutants to study the etioplast-chloroplast transition</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>In angiosperm plants, the etioplast-chloroplast transition is light-dependent. A key factor in this process is the protochlorophyllide oxidoreductase A (PORA), which catalyzes the light-induced reduction of protochlorophyllide to chlorophyllide. The import pathway of the precursor protein prePORA into chloroplasts was analyzed in vivo and in vitro by using homozygous loss-of-function mutants in genes coding for chlorophyllide a oxygenase (CAO) or for members of the outer-envelope solute-channel protein family of 16 kDa (OEP16), both of which have been implied to be key factors for the import of prePORA. Our in vivo analyses show that cao or oep16 mutants contain a normally structured prolamellar body that contains the protochlorophyllide holochrome. Furthermore, etioplasts from cao and oep16 mutants contain PORA protein as found by mass spectrometry. Our data demonstrate that both CAO and OEP16 are dispensable for chloroplast biogenesis and play no central role in the import of prePORA in vivo and in vitro as further indicated by protein import studies.</description><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis - radiation effects</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Arabidopsis thaliana</subject><subject>Base Sequence</subject><subject>Biological Sciences</subject><subject>Chlorophyll</subject><subject>chlorophyllide a oxygenase</subject><subject>Chlorophyllides - metabolism</subject><subject>chloroplast biogenesis</subject><subject>Chloroplasts</subject><subject>Chloroplasts - genetics</subject><subject>Chloroplasts - metabolism</subject><subject>Chloroplasts - radiation effects</subject><subject>Cotyledons</subject><subject>cytochemistry</subject><subject>DNA Primers - genetics</subject><subject>Etioplasts</subject><subject>Genes</subject><subject>Genes, Plant</subject><subject>Imports</subject><subject>Ion Channels - genetics</subject><subject>Ion Channels - metabolism</subject><subject>mutants</subject><subject>Mutation</subject><subject>oxidoreductases</subject><subject>oxygenases</subject><subject>Oxygenases - genetics</subject><subject>Oxygenases - metabolism</subject><subject>phenotype</subject><subject>Photobiology</subject><subject>Plants</subject><subject>Plastids</subject><subject>Protein isoforms</subject><subject>Protein precursors</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>Protochlorophyllide - metabolism</subject><subject>protochlorophyllide oxidoreductase A</subject><subject>Seedlings</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1vEzEUxC0EoqFw5gSsOHDb9vnZa-9yQKoivqRKHGglbpbjfZtstFkH24vof19HiZrAAU4-zG9G8zyMveRwwUGLy-1o4wUoDqCQg3zEZhwaXirZwGM2A0Bd1hLlGXsW4xoAmqqGp-yMawTEqpqxH_PV4IPfDjamYtH7JY0U-_i-uFlRMUUqfFdspmTHFIvki5im9q5IWaPU712lO0lIwY6xz9L4nD3p7BDpxeE9Z7efPt7Mv5TX3z5_nV9dl05xmUrJRdvWXWWdprqmBlGjJnRV6xaIHKt6AQ44NSS0VtDqSkreOVCiIa21FOfswz53Oy021Doac4fBbEO_seHOeNubP5WxX5ml_2W4VkpKkQPeHQKC_zlRTGbTR0fDYEfyUzSqllwC_h_kTSWaWmEG3_4Frv0UxvwLBoFLRJSQocs95IKPMVD3UJmD2W1rdtua47bZ8fr00iN_GPOk4M55jJMGjdK16aZhSPQ7ZfDVv8Cjvo7JhwcAK4mKK571N3u9s97YZeijuf2eTxOQe-c2QtwDu_LKhQ</recordid><startdate>20070109</startdate><enddate>20070109</enddate><creator>Philippar, Katrin</creator><creator>Geis, Tina</creator><creator>Ilkavets, Iryna</creator><creator>Oster, Ulrike</creator><creator>Schwenkert, Serena</creator><creator>Meurer, Jörg</creator><creator>Soll, Jürgen</creator><general>National Academy of Sciences</general><general>National Acad Sciences</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>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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20070109</creationdate><title>Chloroplast biogenesis: The use of mutants to study the etioplast-chloroplast transition</title><author>Philippar, Katrin ; 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A key factor in this process is the protochlorophyllide oxidoreductase A (PORA), which catalyzes the light-induced reduction of protochlorophyllide to chlorophyllide. The import pathway of the precursor protein prePORA into chloroplasts was analyzed in vivo and in vitro by using homozygous loss-of-function mutants in genes coding for chlorophyllide a oxygenase (CAO) or for members of the outer-envelope solute-channel protein family of 16 kDa (OEP16), both of which have been implied to be key factors for the import of prePORA. Our in vivo analyses show that cao or oep16 mutants contain a normally structured prolamellar body that contains the protochlorophyllide holochrome. Furthermore, etioplasts from cao and oep16 mutants contain PORA protein as found by mass spectrometry. Our data demonstrate that both CAO and OEP16 are dispensable for chloroplast biogenesis and play no central role in the import of prePORA in vivo and in vitro as further indicated by protein import studies.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>17202255</pmid><doi>10.1073/pnas.0610062104</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis - radiation effects Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Arabidopsis thaliana Base Sequence Biological Sciences Chlorophyll chlorophyllide a oxygenase Chlorophyllides - metabolism chloroplast biogenesis Chloroplasts Chloroplasts - genetics Chloroplasts - metabolism Chloroplasts - radiation effects Cotyledons cytochemistry DNA Primers - genetics Etioplasts Genes Genes, Plant Imports Ion Channels - genetics Ion Channels - metabolism mutants Mutation oxidoreductases oxygenases Oxygenases - genetics Oxygenases - metabolism phenotype Photobiology Plants Plastids Protein isoforms Protein precursors Protein Transport Proteins Protochlorophyllide - metabolism protochlorophyllide oxidoreductase A Seedlings |
| title | Chloroplast biogenesis: The use of mutants to study the etioplast-chloroplast transition |
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