Substrate channeling in oxylipin biosynthesis through a protein complex in the plastid envelope of Arabidopsis thaliana
13 Pág.
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| Format: | artículo biblioteca |
| Language: | English |
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Oxford University Press
2019-03-11
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| Subjects: | Allene oxide synthase, Allene oxide cyclase, Chloroplast envelope protein complex, Hydroperoxide lyase, Lipoxygenase, Metabolite channeling, Plant defense, |
| Online Access: | http://hdl.handle.net/10261/367511 http://dx.doi.org/10.13039/501100011033 http://dx.doi.org/10.13039/501100010198 http://dx.doi.org/10.13039/501100001659 http://dx.doi.org/10.13039/501100000780 https://api.elsevier.com/content/abstract/scopus_id/85062868716 |
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dig-inia-es-10261-3675112024-10-28T21:37:24Z Substrate channeling in oxylipin biosynthesis through a protein complex in the plastid envelope of Arabidopsis thaliana Pollmann, Stephan Springer, Armin Rustgi, Sachin von Wettstein, Diter Kang, ChulHee Reinbothe, Christiane Reinbothe, Steffen European Commission German Research Foundation Ministerio de Economía, Industria y Competitividad (España) Agencia Estatal de Investigación (España) Pollmann, Stephan [0000-0002-5111-4425] Springer, Armin [0000-0001-9878-7240] Rustgi, Sachin [0000-0002-6881-9501] von Wettstein, Diter [0000-0002-4393-6920] Kang, ChulHee [0000-0002-0693-7860] Reinbothe, Christiane [0009-0008-1863-0138] Reinbothe, Steffen [0000-0002-9701-3267] Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72] Allene oxide synthase Allene oxide cyclase Chloroplast envelope protein complex Hydroperoxide lyase Lipoxygenase Metabolite channeling Plant defense 13 Pág. Oxygenated membrane fatty acid derivatives termed oxylipins play important roles in plant defense against biotic and abiotic cues. Plants challenged by insect pests, for example, synthesize a blend of different defense compounds that include volatile aldehydes and jasmonic acid (JA), among others. Because all oxylipins are derived from the same pathway, we investigated how their synthesis might be regulated, focusing on two closely related atypical cytochrome P450 enzymes designated CYP74A and CYP74B, respectively, allene oxide synthase (AOS) and hydroperoxide lyase (HPL). These enzymes compete for the same substrate but give rise to different products: the final product of the AOS branch of the oxylipin pathway is JA, while those of the HPL branch comprise volatile aldehydes and alcohols. AOS and HPL are plastid envelope enzymes in Arabidopsis thaliana but accumulate at different locations. Biochemical experiments identified AOS as a constituent of complexes also containing lipoxygenase 2 (LOX2) and allene oxide cyclase (AOC), which catalyze consecutive steps in JA precursor biosynthesis, while excluding the concurrent HPL reaction. Based on published X-ray data, the structure of this complex was modelled and amino acids involved in catalysis and subunit interactions predicted. Genetic studies identified the microRNA 319-regulated clade of TCP (TEOSINTE BRANCHED/CYCLOIDEA/PCF) transcription factor genes and CORONATINE INSENSITIVE 1 (COI1) as controlling JA production through the LOX2-AOS-AOC2 complex. Together, our results define a molecular branch point in oxylipin biosynthesis that allows fine-tuning of the plant's defense machinery in response to biotic and abiotic stimuli. This work was supported by a Marie Curie grant of the European Commission (FP7-PEOPLE-CIG-2011–303744), a grant from the German Science Foundation (PO1214/3-2), and a grant from the Spanish Ministry of Economy, Industry and Competiveness (BFU2017-82826-R) to SP. Peer reviewed 2024-09-11T12:29:15Z 2024-09-11T12:29:15Z 2019-03-11 artículo http://purl.org/coar/resource_type/c_6501 Journal of Experimental Botany 70(5): 1483-1495 (2019) 0022-0957 http://hdl.handle.net/10261/367511 10.1093/jxb/erz015 1460-2431 http://dx.doi.org/10.13039/501100011033 http://dx.doi.org/10.13039/501100010198 http://dx.doi.org/10.13039/501100001659 http://dx.doi.org/10.13039/501100000780 30690555 2-s2.0-85062868716 https://api.elsevier.com/content/abstract/scopus_id/85062868716 en #PLACEHOLDER_PARENT_METADATA_VALUE# #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/EC/FP7/303744 info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BFU2017-82826-R/ES/ACLARACION DE LOS MECANISMOS MOLECULARES CONECTANDO EL NUDO AMI1 CON EL EQUILIBRIO ENTRE CRECIMIENTO Y DEFENSA/ Centro de Biotecnología y Genómica de Plantas (CBGP) Publisher's version https://doi.org/10.1093/jxb/erz015 Sí open application/pdf Oxford University Press |
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Allene oxide synthase Allene oxide cyclase Chloroplast envelope protein complex Hydroperoxide lyase Lipoxygenase Metabolite channeling Plant defense Allene oxide synthase Allene oxide cyclase Chloroplast envelope protein complex Hydroperoxide lyase Lipoxygenase Metabolite channeling Plant defense |
| spellingShingle |
Allene oxide synthase Allene oxide cyclase Chloroplast envelope protein complex Hydroperoxide lyase Lipoxygenase Metabolite channeling Plant defense Allene oxide synthase Allene oxide cyclase Chloroplast envelope protein complex Hydroperoxide lyase Lipoxygenase Metabolite channeling Plant defense Pollmann, Stephan Springer, Armin Rustgi, Sachin von Wettstein, Diter Kang, ChulHee Reinbothe, Christiane Reinbothe, Steffen Substrate channeling in oxylipin biosynthesis through a protein complex in the plastid envelope of Arabidopsis thaliana |
| description |
13 Pág. |
| author2 |
European Commission |
| author_facet |
European Commission Pollmann, Stephan Springer, Armin Rustgi, Sachin von Wettstein, Diter Kang, ChulHee Reinbothe, Christiane Reinbothe, Steffen |
| format |
artículo |
| topic_facet |
Allene oxide synthase Allene oxide cyclase Chloroplast envelope protein complex Hydroperoxide lyase Lipoxygenase Metabolite channeling Plant defense |
| author |
Pollmann, Stephan Springer, Armin Rustgi, Sachin von Wettstein, Diter Kang, ChulHee Reinbothe, Christiane Reinbothe, Steffen |
| author_sort |
Pollmann, Stephan |
| title |
Substrate channeling in oxylipin biosynthesis through a protein complex in the plastid envelope of Arabidopsis thaliana |
| title_short |
Substrate channeling in oxylipin biosynthesis through a protein complex in the plastid envelope of Arabidopsis thaliana |
| title_full |
Substrate channeling in oxylipin biosynthesis through a protein complex in the plastid envelope of Arabidopsis thaliana |
| title_fullStr |
Substrate channeling in oxylipin biosynthesis through a protein complex in the plastid envelope of Arabidopsis thaliana |
| title_full_unstemmed |
Substrate channeling in oxylipin biosynthesis through a protein complex in the plastid envelope of Arabidopsis thaliana |
| title_sort |
substrate channeling in oxylipin biosynthesis through a protein complex in the plastid envelope of arabidopsis thaliana |
| publisher |
Oxford University Press |
| publishDate |
2019-03-11 |
| url |
http://hdl.handle.net/10261/367511 http://dx.doi.org/10.13039/501100011033 http://dx.doi.org/10.13039/501100010198 http://dx.doi.org/10.13039/501100001659 http://dx.doi.org/10.13039/501100000780 https://api.elsevier.com/content/abstract/scopus_id/85062868716 |
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1816136721197170688 |