A Role for Chlorophyllide a Oxygenase in the Regulated Import and Stabilization of Light-Harvesting Chlorophyll a/b Proteins
The Arabidopsis CAO gene encodes a 52-kDa protein with predicted localization in the plastid compartment. Here, we report that CAO is an intrinsic Rieske iron-sulfur protein of the plastidenvelope inner and thylakoid membranes. Activity measurements revealed that CAO catalyzes chlorophyllide a to ch...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2006-03, Vol.103 (12), p.4777-4782 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Reinbothe, Christiane Bartsch, Sandra Eggink, Laura L. Hoober, J. Kenneth Brusslan, Judy Andrade-Paz, Ricardo Monnet, Julie Reinbothe, Steffen |
| description | The Arabidopsis CAO gene encodes a 52-kDa protein with predicted localization in the plastid compartment. Here, we report that CAO is an intrinsic Rieske iron-sulfur protein of the plastidenvelope inner and thylakoid membranes. Activity measurements revealed that CAO catalyzes chlorophyllide a to chlorophyllide b conversion in vitro and that the enzyme was only slightly active with protochlorophyllide a, the nonreduced precursor of chlorophyllide a. Protein import and organelle fractionation studies identified CAO to be distinct from Ptc52 in the substrate-dependent transport pathway of NADPH:protochlorophyllide oxidoreductase A but instead to be part of a separate translocon complex. This complex was involved in the regulated import and stabilization of the chlorophyllide b-binding light-harvesting proteins Lhcbl (LHCII) and Lhcb4 (CP29) in chloroplasts. Together, our results provide insights into the plastid subcompartmentalization and evolution of chlorophyll precursor biosynthesis in relation to protein import in higher plants. |
| doi_str_mv | 10.1073/pnas.0511066103 |
| format | Article |
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Kenneth ; Brusslan, Judy ; Andrade-Paz, Ricardo ; Monnet, Julie ; Reinbothe, Steffen</creator><creatorcontrib>Reinbothe, Christiane ; Bartsch, Sandra ; Eggink, Laura L. ; Hoober, J. Kenneth ; Brusslan, Judy ; Andrade-Paz, Ricardo ; Monnet, Julie ; Reinbothe, Steffen</creatorcontrib><description>The Arabidopsis CAO gene encodes a 52-kDa protein with predicted localization in the plastid compartment. Here, we report that CAO is an intrinsic Rieske iron-sulfur protein of the plastidenvelope inner and thylakoid membranes. Activity measurements revealed that CAO catalyzes chlorophyllide a to chlorophyllide b conversion in vitro and that the enzyme was only slightly active with protochlorophyllide a, the nonreduced precursor of chlorophyllide a. Protein import and organelle fractionation studies identified CAO to be distinct from Ptc52 in the substrate-dependent transport pathway of NADPH:protochlorophyllide oxidoreductase A but instead to be part of a separate translocon complex. This complex was involved in the regulated import and stabilization of the chlorophyllide b-binding light-harvesting proteins Lhcbl (LHCII) and Lhcb4 (CP29) in chloroplasts. Together, our results provide insights into the plastid subcompartmentalization and evolution of chlorophyll precursor biosynthesis in relation to protein import in higher plants.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0511066103</identifier><identifier>PMID: 16537436</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Arabidopsis ; Arabidopsis - enzymology ; Arabidopsis - genetics ; Barley ; Biochemistry, Molecular Biology ; Biological Sciences ; Chlorophyll ; Chlorophyllides ; Chlorophyllides - metabolism ; Chlorophylls ; Chloroplasts ; Crosslinking ; Electron Transport Complex III - genetics ; Electron Transport Complex III - metabolism ; Enzyme Stability ; Enzymes ; Flowers & plants ; Genes ; Imports ; Iron-Sulfur Proteins - genetics ; Iron-Sulfur Proteins - metabolism ; Life Sciences ; Light-Harvesting Protein Complexes - metabolism ; Oxygenases - genetics ; Oxygenases - metabolism ; P branes ; Photosystem II Protein Complex - metabolism ; Pigments ; Plastids ; Protein Kinases - metabolism ; Protein precursors ; Protein Transport ; Proteins ; Thylakoids - enzymology</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2006-03, Vol.103 (12), p.4777-4782</ispartof><rights>Copyright 2006 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Mar 21, 2006</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>2006 by The National Academy of Sciences of the USA 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c562t-6b05ebd7e53301f3312c0724b762d3e5b0489190613c2bcd8e641cd6317015983</citedby><cites>FETCH-LOGICAL-c562t-6b05ebd7e53301f3312c0724b762d3e5b0489190613c2bcd8e641cd6317015983</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/103/12.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/30049017$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/30049017$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,724,777,781,800,882,27905,27906,53772,53774,57998,58231</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16537436$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00084597$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Reinbothe, Christiane</creatorcontrib><creatorcontrib>Bartsch, Sandra</creatorcontrib><creatorcontrib>Eggink, Laura L.</creatorcontrib><creatorcontrib>Hoober, J. Kenneth</creatorcontrib><creatorcontrib>Brusslan, Judy</creatorcontrib><creatorcontrib>Andrade-Paz, Ricardo</creatorcontrib><creatorcontrib>Monnet, Julie</creatorcontrib><creatorcontrib>Reinbothe, Steffen</creatorcontrib><title>A Role for Chlorophyllide a Oxygenase in the Regulated Import and Stabilization of Light-Harvesting Chlorophyll a/b Proteins</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The Arabidopsis CAO gene encodes a 52-kDa protein with predicted localization in the plastid compartment. Here, we report that CAO is an intrinsic Rieske iron-sulfur protein of the plastidenvelope inner and thylakoid membranes. Activity measurements revealed that CAO catalyzes chlorophyllide a to chlorophyllide b conversion in vitro and that the enzyme was only slightly active with protochlorophyllide a, the nonreduced precursor of chlorophyllide a. Protein import and organelle fractionation studies identified CAO to be distinct from Ptc52 in the substrate-dependent transport pathway of NADPH:protochlorophyllide oxidoreductase A but instead to be part of a separate translocon complex. This complex was involved in the regulated import and stabilization of the chlorophyllide b-binding light-harvesting proteins Lhcbl (LHCII) and Lhcb4 (CP29) in chloroplasts. 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Kenneth</au><au>Brusslan, Judy</au><au>Andrade-Paz, Ricardo</au><au>Monnet, Julie</au><au>Reinbothe, Steffen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Role for Chlorophyllide a Oxygenase in the Regulated Import and Stabilization of Light-Harvesting Chlorophyll a/b Proteins</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2006-03-21</date><risdate>2006</risdate><volume>103</volume><issue>12</issue><spage>4777</spage><epage>4782</epage><pages>4777-4782</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The Arabidopsis CAO gene encodes a 52-kDa protein with predicted localization in the plastid compartment. Here, we report that CAO is an intrinsic Rieske iron-sulfur protein of the plastidenvelope inner and thylakoid membranes. Activity measurements revealed that CAO catalyzes chlorophyllide a to chlorophyllide b conversion in vitro and that the enzyme was only slightly active with protochlorophyllide a, the nonreduced precursor of chlorophyllide a. Protein import and organelle fractionation studies identified CAO to be distinct from Ptc52 in the substrate-dependent transport pathway of NADPH:protochlorophyllide oxidoreductase A but instead to be part of a separate translocon complex. This complex was involved in the regulated import and stabilization of the chlorophyllide b-binding light-harvesting proteins Lhcbl (LHCII) and Lhcb4 (CP29) in chloroplasts. 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| subjects | Arabidopsis Arabidopsis - enzymology Arabidopsis - genetics Barley Biochemistry, Molecular Biology Biological Sciences Chlorophyll Chlorophyllides Chlorophyllides - metabolism Chlorophylls Chloroplasts Crosslinking Electron Transport Complex III - genetics Electron Transport Complex III - metabolism Enzyme Stability Enzymes Flowers & plants Genes Imports Iron-Sulfur Proteins - genetics Iron-Sulfur Proteins - metabolism Life Sciences Light-Harvesting Protein Complexes - metabolism Oxygenases - genetics Oxygenases - metabolism P branes Photosystem II Protein Complex - metabolism Pigments Plastids Protein Kinases - metabolism Protein precursors Protein Transport Proteins Thylakoids - enzymology |
| title | A Role for Chlorophyllide a Oxygenase in the Regulated Import and Stabilization of Light-Harvesting Chlorophyll a/b Proteins |
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