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  JASSY, a chloroplast outer membrane protein required for jasmonate biosynthesis.

Guan, L., Denkert, N., Eisa, A., Lehmann, M., Sjuts, I., Weiberg, A., et al. (2019). JASSY, a chloroplast outer membrane protein required for jasmonate biosynthesis. Proceedings of the National Academy of Sciences of the United States of America, 116(21), 10568-10575. doi:10.1073/pnas.1900482116.

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 Creators:
Guan, L., Author
Denkert, N.1, Author           
Eisa, A., Author
Lehmann, M., Author
Sjuts, I., Author
Weiberg, A., Author
Soll, J., Author
Meinecke, M., Author
Schwenkert, S., Author
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1Research Group of Membrane Protein Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_2149675              

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Free keywords: jasmonate; plant hormones; chloroplast; membrane pore; cold acclimation
 Abstract: Jasmonates are vital plant hormones that not only act in the stress response to biotic and abiotic influences, such as wounding, pathogen attack, and cold acclimation, but also drive developmental processes in cooperation with other plant hormones. The biogenesis of jasmonates starts in the chloroplast, where several enzymatic steps produce the jasmonate precursor 12-oxophytodienoic acid (OPDA) from alpha-linolenic acid. OPDA in turn is exported into the cytosol for further conversion into active jasmonates, which subsequently induces the expression of multiple genes in the nucleus. Despite its obvious importance, the export of OPDA across the chloroplast membranes has remained elusive. In this study, we characterized a protein residing in the chloroplast outer membrane, JASSY, which has proven indispensable for the export of OPDA from the chloroplast. We provide evidence that JASSY has channel-like properties and propose that it thereby facilitates OPDA transport. Consequently, a lack of JASSY in Arabidopsis leads to a deficiency in accumulation of jasmonic acids, which results in impaired expression of jasmonate target genes on exposure to various stresses. This results in plants that are more susceptible to pathogen attack and also exhibit defects in cold acclimation.

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Language(s): eng - English
 Dates: 2019-05-21
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.1900482116
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
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Pages: - Volume / Issue: 116 (21) Sequence Number: - Start / End Page: 10568 - 10575 Identifier: -