Water-soluble chlorophyll protein is involved in herbivore resistance activation during greening of Arabidopsis thaliana
Water-soluble chlorophyll proteins (WSCPs) constitute a small family of unusual chlorophyll (Chl)-binding proteins that possess a Kunitz-type protease inhibitor domain. In Arabidopsis thaliana, a WSCP has been identified, named AtWSCP, that forms complexes with Chl and the Chl precursor chlorophylli...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Diter von Wettstein [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Rechteinformationen: |
Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences |
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| Übergeordnetes Werk: |
Enthalten in: Proceedings of the National Academy of Sciences of the United States of America - Washington, DC : NAS, 1877, 112(2015), 23, Seite 7303 |
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| Übergeordnetes Werk: |
volume:112 ; year:2015 ; number:23 ; pages:7303 |
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|---|
| DOI / URN: |
10.1073/pnas.1507714112 |
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| 520 | |a Water-soluble chlorophyll proteins (WSCPs) constitute a small family of unusual chlorophyll (Chl)-binding proteins that possess a Kunitz-type protease inhibitor domain. In Arabidopsis thaliana, a WSCP has been identified, named AtWSCP, that forms complexes with Chl and the Chl precursor chlorophyllide (Chlide) in vitro. AtWSCP exhibits a quite unexpected expression pattern for a Chl binding protein and accumulated to high levels in the apical hook of etiolated plants. AtWSCP expression was negatively light-regulated. Transgenic expression of AtWSCP fused to green fluorescent protein (GFP) revealed that AtWSCP is localized to cell walls/apoplastic spaces. Biochemical assays identified AtWSCP as interacting with RD21 (responsive to desiccation 21), a granulin domain-containing cysteine protease implicated in stress responses and defense. Reconstitution experiments showed tight interactions between RD21 and WSCP that were relieved upon Chlide binding. Laboratory feeding experiments with two herbivorous isopod crustaceans, Porcellio scaber (woodlouse) and Armadillidium vulgare (pillbug), identified the apical hook as Achilles' heel of etiolated plants and that this was protected by RD21 during greening. Because Chlide is formed in the apical hook during seedling emergence from the soil, our data suggest an unprecedented mechanism of herbivore resistance activation that is triggered by light and involves AtWSCP. | ||
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| 650 | 4 | |a Chlorophyll Binding Proteins - metabolism | |
| 650 | 4 | |a Hypocotyl - growth & development | |
| 650 | 4 | |a Chlorophyll Binding Proteins - physiology | |
| 650 | 4 | |a Arabidopsis - physiology | |
| 650 | 4 | |a Arabidopsis Proteins - physiology | |
| 650 | 4 | |a Cysteine Proteases - metabolism | |
| 650 | 4 | |a Arabidopsis Proteins - metabolism | |
| 650 | 4 | |a Arabidopsis Proteins - genetics | |
| 650 | 4 | |a Chlorophyll Binding Proteins - genetics | |
| 650 | 4 | |a Chlorophyll | |
| 650 | 4 | |a Plant proteins | |
| 650 | 4 | |a Arabidopsis thaliana | |
| 650 | 4 | |a Physiological aspects | |
| 650 | 4 | |a Flowers & plants | |
| 650 | 4 | |a Proteins | |
| 650 | 4 | |a Herbivores | |
| 650 | 4 | |a Crustaceans | |
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| 700 | 0 | |a Edouard Boex-Fontvieille |4 oth | |
| 700 | 0 | |a Sachin Rustgi |4 oth | |
| 700 | 0 | |a Steffen Reinbothe |4 oth | |
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10.1073/pnas.1507714112 doi PQ20160211 (DE-627)OLC1970273224 (DE-599)GBVOLC1970273224 (PRQ)g1818-a3e6167de3a25352ca6a6af3dde95ab593e7c36477e932abe628fda995cb87563 (KEY)0583363920150000112002307303watersolublechlorophyllproteinisinvolvedinherbivor DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Diter von Wettstein verfasserin aut Water-soluble chlorophyll protein is involved in herbivore resistance activation during greening of Arabidopsis thaliana 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Water-soluble chlorophyll proteins (WSCPs) constitute a small family of unusual chlorophyll (Chl)-binding proteins that possess a Kunitz-type protease inhibitor domain. In Arabidopsis thaliana, a WSCP has been identified, named AtWSCP, that forms complexes with Chl and the Chl precursor chlorophyllide (Chlide) in vitro. AtWSCP exhibits a quite unexpected expression pattern for a Chl binding protein and accumulated to high levels in the apical hook of etiolated plants. AtWSCP expression was negatively light-regulated. Transgenic expression of AtWSCP fused to green fluorescent protein (GFP) revealed that AtWSCP is localized to cell walls/apoplastic spaces. Biochemical assays identified AtWSCP as interacting with RD21 (responsive to desiccation 21), a granulin domain-containing cysteine protease implicated in stress responses and defense. Reconstitution experiments showed tight interactions between RD21 and WSCP that were relieved upon Chlide binding. Laboratory feeding experiments with two herbivorous isopod crustaceans, Porcellio scaber (woodlouse) and Armadillidium vulgare (pillbug), identified the apical hook as Achilles' heel of etiolated plants and that this was protected by RD21 during greening. Because Chlide is formed in the apical hook during seedling emergence from the soil, our data suggest an unprecedented mechanism of herbivore resistance activation that is triggered by light and involves AtWSCP. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Chlorophyll Binding Proteins - metabolism Hypocotyl - growth & development Chlorophyll Binding Proteins - physiology Arabidopsis - physiology Arabidopsis Proteins - physiology Cysteine Proteases - metabolism Arabidopsis Proteins - metabolism Arabidopsis Proteins - genetics Chlorophyll Binding Proteins - genetics Chlorophyll Plant proteins Arabidopsis thaliana Physiological aspects Flowers & plants Proteins Herbivores Crustaceans Christiane Reinbothe oth Edouard Boex-Fontvieille oth Sachin Rustgi oth Steffen Reinbothe oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 23, Seite 7303 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:23 pages:7303 http://dx.doi.org/10.1073/pnas.1507714112 Volltext http://www.pnas.org/content/112/23/7303.abstract http://www.ncbi.nlm.nih.gov/pubmed/26016527 http://search.proquest.com/docview/1691074660 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 23 7303 |
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10.1073/pnas.1507714112 doi PQ20160211 (DE-627)OLC1970273224 (DE-599)GBVOLC1970273224 (PRQ)g1818-a3e6167de3a25352ca6a6af3dde95ab593e7c36477e932abe628fda995cb87563 (KEY)0583363920150000112002307303watersolublechlorophyllproteinisinvolvedinherbivor DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Diter von Wettstein verfasserin aut Water-soluble chlorophyll protein is involved in herbivore resistance activation during greening of Arabidopsis thaliana 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Water-soluble chlorophyll proteins (WSCPs) constitute a small family of unusual chlorophyll (Chl)-binding proteins that possess a Kunitz-type protease inhibitor domain. In Arabidopsis thaliana, a WSCP has been identified, named AtWSCP, that forms complexes with Chl and the Chl precursor chlorophyllide (Chlide) in vitro. AtWSCP exhibits a quite unexpected expression pattern for a Chl binding protein and accumulated to high levels in the apical hook of etiolated plants. AtWSCP expression was negatively light-regulated. Transgenic expression of AtWSCP fused to green fluorescent protein (GFP) revealed that AtWSCP is localized to cell walls/apoplastic spaces. Biochemical assays identified AtWSCP as interacting with RD21 (responsive to desiccation 21), a granulin domain-containing cysteine protease implicated in stress responses and defense. Reconstitution experiments showed tight interactions between RD21 and WSCP that were relieved upon Chlide binding. Laboratory feeding experiments with two herbivorous isopod crustaceans, Porcellio scaber (woodlouse) and Armadillidium vulgare (pillbug), identified the apical hook as Achilles' heel of etiolated plants and that this was protected by RD21 during greening. Because Chlide is formed in the apical hook during seedling emergence from the soil, our data suggest an unprecedented mechanism of herbivore resistance activation that is triggered by light and involves AtWSCP. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Chlorophyll Binding Proteins - metabolism Hypocotyl - growth & development Chlorophyll Binding Proteins - physiology Arabidopsis - physiology Arabidopsis Proteins - physiology Cysteine Proteases - metabolism Arabidopsis Proteins - metabolism Arabidopsis Proteins - genetics Chlorophyll Binding Proteins - genetics Chlorophyll Plant proteins Arabidopsis thaliana Physiological aspects Flowers & plants Proteins Herbivores Crustaceans Christiane Reinbothe oth Edouard Boex-Fontvieille oth Sachin Rustgi oth Steffen Reinbothe oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 23, Seite 7303 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:23 pages:7303 http://dx.doi.org/10.1073/pnas.1507714112 Volltext http://www.pnas.org/content/112/23/7303.abstract http://www.ncbi.nlm.nih.gov/pubmed/26016527 http://search.proquest.com/docview/1691074660 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 23 7303 |
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10.1073/pnas.1507714112 doi PQ20160211 (DE-627)OLC1970273224 (DE-599)GBVOLC1970273224 (PRQ)g1818-a3e6167de3a25352ca6a6af3dde95ab593e7c36477e932abe628fda995cb87563 (KEY)0583363920150000112002307303watersolublechlorophyllproteinisinvolvedinherbivor DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Diter von Wettstein verfasserin aut Water-soluble chlorophyll protein is involved in herbivore resistance activation during greening of Arabidopsis thaliana 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Water-soluble chlorophyll proteins (WSCPs) constitute a small family of unusual chlorophyll (Chl)-binding proteins that possess a Kunitz-type protease inhibitor domain. In Arabidopsis thaliana, a WSCP has been identified, named AtWSCP, that forms complexes with Chl and the Chl precursor chlorophyllide (Chlide) in vitro. AtWSCP exhibits a quite unexpected expression pattern for a Chl binding protein and accumulated to high levels in the apical hook of etiolated plants. AtWSCP expression was negatively light-regulated. Transgenic expression of AtWSCP fused to green fluorescent protein (GFP) revealed that AtWSCP is localized to cell walls/apoplastic spaces. Biochemical assays identified AtWSCP as interacting with RD21 (responsive to desiccation 21), a granulin domain-containing cysteine protease implicated in stress responses and defense. Reconstitution experiments showed tight interactions between RD21 and WSCP that were relieved upon Chlide binding. Laboratory feeding experiments with two herbivorous isopod crustaceans, Porcellio scaber (woodlouse) and Armadillidium vulgare (pillbug), identified the apical hook as Achilles' heel of etiolated plants and that this was protected by RD21 during greening. Because Chlide is formed in the apical hook during seedling emergence from the soil, our data suggest an unprecedented mechanism of herbivore resistance activation that is triggered by light and involves AtWSCP. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Chlorophyll Binding Proteins - metabolism Hypocotyl - growth & development Chlorophyll Binding Proteins - physiology Arabidopsis - physiology Arabidopsis Proteins - physiology Cysteine Proteases - metabolism Arabidopsis Proteins - metabolism Arabidopsis Proteins - genetics Chlorophyll Binding Proteins - genetics Chlorophyll Plant proteins Arabidopsis thaliana Physiological aspects Flowers & plants Proteins Herbivores Crustaceans Christiane Reinbothe oth Edouard Boex-Fontvieille oth Sachin Rustgi oth Steffen Reinbothe oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 23, Seite 7303 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:23 pages:7303 http://dx.doi.org/10.1073/pnas.1507714112 Volltext http://www.pnas.org/content/112/23/7303.abstract http://www.ncbi.nlm.nih.gov/pubmed/26016527 http://search.proquest.com/docview/1691074660 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 23 7303 |
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10.1073/pnas.1507714112 doi PQ20160211 (DE-627)OLC1970273224 (DE-599)GBVOLC1970273224 (PRQ)g1818-a3e6167de3a25352ca6a6af3dde95ab593e7c36477e932abe628fda995cb87563 (KEY)0583363920150000112002307303watersolublechlorophyllproteinisinvolvedinherbivor DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Diter von Wettstein verfasserin aut Water-soluble chlorophyll protein is involved in herbivore resistance activation during greening of Arabidopsis thaliana 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Water-soluble chlorophyll proteins (WSCPs) constitute a small family of unusual chlorophyll (Chl)-binding proteins that possess a Kunitz-type protease inhibitor domain. In Arabidopsis thaliana, a WSCP has been identified, named AtWSCP, that forms complexes with Chl and the Chl precursor chlorophyllide (Chlide) in vitro. AtWSCP exhibits a quite unexpected expression pattern for a Chl binding protein and accumulated to high levels in the apical hook of etiolated plants. AtWSCP expression was negatively light-regulated. Transgenic expression of AtWSCP fused to green fluorescent protein (GFP) revealed that AtWSCP is localized to cell walls/apoplastic spaces. Biochemical assays identified AtWSCP as interacting with RD21 (responsive to desiccation 21), a granulin domain-containing cysteine protease implicated in stress responses and defense. Reconstitution experiments showed tight interactions between RD21 and WSCP that were relieved upon Chlide binding. Laboratory feeding experiments with two herbivorous isopod crustaceans, Porcellio scaber (woodlouse) and Armadillidium vulgare (pillbug), identified the apical hook as Achilles' heel of etiolated plants and that this was protected by RD21 during greening. Because Chlide is formed in the apical hook during seedling emergence from the soil, our data suggest an unprecedented mechanism of herbivore resistance activation that is triggered by light and involves AtWSCP. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Chlorophyll Binding Proteins - metabolism Hypocotyl - growth & development Chlorophyll Binding Proteins - physiology Arabidopsis - physiology Arabidopsis Proteins - physiology Cysteine Proteases - metabolism Arabidopsis Proteins - metabolism Arabidopsis Proteins - genetics Chlorophyll Binding Proteins - genetics Chlorophyll Plant proteins Arabidopsis thaliana Physiological aspects Flowers & plants Proteins Herbivores Crustaceans Christiane Reinbothe oth Edouard Boex-Fontvieille oth Sachin Rustgi oth Steffen Reinbothe oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 23, Seite 7303 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:23 pages:7303 http://dx.doi.org/10.1073/pnas.1507714112 Volltext http://www.pnas.org/content/112/23/7303.abstract http://www.ncbi.nlm.nih.gov/pubmed/26016527 http://search.proquest.com/docview/1691074660 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 23 7303 |
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10.1073/pnas.1507714112 doi PQ20160211 (DE-627)OLC1970273224 (DE-599)GBVOLC1970273224 (PRQ)g1818-a3e6167de3a25352ca6a6af3dde95ab593e7c36477e932abe628fda995cb87563 (KEY)0583363920150000112002307303watersolublechlorophyllproteinisinvolvedinherbivor DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Diter von Wettstein verfasserin aut Water-soluble chlorophyll protein is involved in herbivore resistance activation during greening of Arabidopsis thaliana 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Water-soluble chlorophyll proteins (WSCPs) constitute a small family of unusual chlorophyll (Chl)-binding proteins that possess a Kunitz-type protease inhibitor domain. In Arabidopsis thaliana, a WSCP has been identified, named AtWSCP, that forms complexes with Chl and the Chl precursor chlorophyllide (Chlide) in vitro. AtWSCP exhibits a quite unexpected expression pattern for a Chl binding protein and accumulated to high levels in the apical hook of etiolated plants. AtWSCP expression was negatively light-regulated. Transgenic expression of AtWSCP fused to green fluorescent protein (GFP) revealed that AtWSCP is localized to cell walls/apoplastic spaces. Biochemical assays identified AtWSCP as interacting with RD21 (responsive to desiccation 21), a granulin domain-containing cysteine protease implicated in stress responses and defense. Reconstitution experiments showed tight interactions between RD21 and WSCP that were relieved upon Chlide binding. Laboratory feeding experiments with two herbivorous isopod crustaceans, Porcellio scaber (woodlouse) and Armadillidium vulgare (pillbug), identified the apical hook as Achilles' heel of etiolated plants and that this was protected by RD21 during greening. Because Chlide is formed in the apical hook during seedling emergence from the soil, our data suggest an unprecedented mechanism of herbivore resistance activation that is triggered by light and involves AtWSCP. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Chlorophyll Binding Proteins - metabolism Hypocotyl - growth & development Chlorophyll Binding Proteins - physiology Arabidopsis - physiology Arabidopsis Proteins - physiology Cysteine Proteases - metabolism Arabidopsis Proteins - metabolism Arabidopsis Proteins - genetics Chlorophyll Binding Proteins - genetics Chlorophyll Plant proteins Arabidopsis thaliana Physiological aspects Flowers & plants Proteins Herbivores Crustaceans Christiane Reinbothe oth Edouard Boex-Fontvieille oth Sachin Rustgi oth Steffen Reinbothe oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 23, Seite 7303 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:23 pages:7303 http://dx.doi.org/10.1073/pnas.1507714112 Volltext http://www.pnas.org/content/112/23/7303.abstract http://www.ncbi.nlm.nih.gov/pubmed/26016527 http://search.proquest.com/docview/1691074660 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 23 7303 |
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water-soluble chlorophyll protein is involved in herbivore resistance activation during greening of arabidopsis thaliana |
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Water-soluble chlorophyll protein is involved in herbivore resistance activation during greening of Arabidopsis thaliana |
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Water-soluble chlorophyll proteins (WSCPs) constitute a small family of unusual chlorophyll (Chl)-binding proteins that possess a Kunitz-type protease inhibitor domain. In Arabidopsis thaliana, a WSCP has been identified, named AtWSCP, that forms complexes with Chl and the Chl precursor chlorophyllide (Chlide) in vitro. AtWSCP exhibits a quite unexpected expression pattern for a Chl binding protein and accumulated to high levels in the apical hook of etiolated plants. AtWSCP expression was negatively light-regulated. Transgenic expression of AtWSCP fused to green fluorescent protein (GFP) revealed that AtWSCP is localized to cell walls/apoplastic spaces. Biochemical assays identified AtWSCP as interacting with RD21 (responsive to desiccation 21), a granulin domain-containing cysteine protease implicated in stress responses and defense. Reconstitution experiments showed tight interactions between RD21 and WSCP that were relieved upon Chlide binding. Laboratory feeding experiments with two herbivorous isopod crustaceans, Porcellio scaber (woodlouse) and Armadillidium vulgare (pillbug), identified the apical hook as Achilles' heel of etiolated plants and that this was protected by RD21 during greening. Because Chlide is formed in the apical hook during seedling emergence from the soil, our data suggest an unprecedented mechanism of herbivore resistance activation that is triggered by light and involves AtWSCP. |
| abstractGer |
Water-soluble chlorophyll proteins (WSCPs) constitute a small family of unusual chlorophyll (Chl)-binding proteins that possess a Kunitz-type protease inhibitor domain. In Arabidopsis thaliana, a WSCP has been identified, named AtWSCP, that forms complexes with Chl and the Chl precursor chlorophyllide (Chlide) in vitro. AtWSCP exhibits a quite unexpected expression pattern for a Chl binding protein and accumulated to high levels in the apical hook of etiolated plants. AtWSCP expression was negatively light-regulated. Transgenic expression of AtWSCP fused to green fluorescent protein (GFP) revealed that AtWSCP is localized to cell walls/apoplastic spaces. Biochemical assays identified AtWSCP as interacting with RD21 (responsive to desiccation 21), a granulin domain-containing cysteine protease implicated in stress responses and defense. Reconstitution experiments showed tight interactions between RD21 and WSCP that were relieved upon Chlide binding. Laboratory feeding experiments with two herbivorous isopod crustaceans, Porcellio scaber (woodlouse) and Armadillidium vulgare (pillbug), identified the apical hook as Achilles' heel of etiolated plants and that this was protected by RD21 during greening. Because Chlide is formed in the apical hook during seedling emergence from the soil, our data suggest an unprecedented mechanism of herbivore resistance activation that is triggered by light and involves AtWSCP. |
| abstract_unstemmed |
Water-soluble chlorophyll proteins (WSCPs) constitute a small family of unusual chlorophyll (Chl)-binding proteins that possess a Kunitz-type protease inhibitor domain. In Arabidopsis thaliana, a WSCP has been identified, named AtWSCP, that forms complexes with Chl and the Chl precursor chlorophyllide (Chlide) in vitro. AtWSCP exhibits a quite unexpected expression pattern for a Chl binding protein and accumulated to high levels in the apical hook of etiolated plants. AtWSCP expression was negatively light-regulated. Transgenic expression of AtWSCP fused to green fluorescent protein (GFP) revealed that AtWSCP is localized to cell walls/apoplastic spaces. Biochemical assays identified AtWSCP as interacting with RD21 (responsive to desiccation 21), a granulin domain-containing cysteine protease implicated in stress responses and defense. Reconstitution experiments showed tight interactions between RD21 and WSCP that were relieved upon Chlide binding. Laboratory feeding experiments with two herbivorous isopod crustaceans, Porcellio scaber (woodlouse) and Armadillidium vulgare (pillbug), identified the apical hook as Achilles' heel of etiolated plants and that this was protected by RD21 during greening. Because Chlide is formed in the apical hook during seedling emergence from the soil, our data suggest an unprecedented mechanism of herbivore resistance activation that is triggered by light and involves AtWSCP. |
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| title_short |
Water-soluble chlorophyll protein is involved in herbivore resistance activation during greening of Arabidopsis thaliana |
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Laboratory feeding experiments with two herbivorous isopod crustaceans, Porcellio scaber (woodlouse) and Armadillidium vulgare (pillbug), identified the apical hook as Achilles' heel of etiolated plants and that this was protected by RD21 during greening. 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metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Arabidopsis Proteins - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Arabidopsis Proteins - genetics</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Chlorophyll Binding Proteins - genetics</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Chlorophyll</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Plant proteins</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Arabidopsis thaliana</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Physiological aspects</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Flowers & plants</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Proteins</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Herbivores</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Crustaceans</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Christiane Reinbothe</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Edouard Boex-Fontvieille</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Sachin Rustgi</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Steffen Reinbothe</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Proceedings of the National Academy of Sciences of the United States of America</subfield><subfield code="d">Washington, DC : NAS, 1877</subfield><subfield code="g">112(2015), 23, Seite 7303</subfield><subfield code="w">(DE-627)129505269</subfield><subfield code="w">(DE-600)209104-5</subfield><subfield code="w">(DE-576)014909189</subfield><subfield code="x">0027-8424</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:112</subfield><subfield code="g">year:2015</subfield><subfield code="g">number:23</subfield><subfield code="g">pages:7303</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">http://dx.doi.org/10.1073/pnas.1507714112</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.pnas.org/content/112/23/7303.abstract</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.ncbi.nlm.nih.gov/pubmed/26016527</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://search.proquest.com/docview/1691074660</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-LING</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-BIODIV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHY</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-MAT</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-FOR</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-DE-84</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-MAT</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-FOR</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_59</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">112</subfield><subfield code="j">2015</subfield><subfield code="e">23</subfield><subfield code="h">7303</subfield></datafield></record></collection>
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