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Genetic manipulation of isoprene emissions in poplar plants remodels the chloroplast proteome.

J. Proteome Res. 13, 2005-2018 (2014)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
Biogenic isoprene (2-methyl-1,3-butadiene) improves the integrity and functionality of thylakoid membranes and scavenges reactive oxygen species (ROS) in plant tissue under stress conditions. On the basis of available physiological studies, we hypothesized that the suppression of isoprene production in the poplar plant by genetic engineering would cause changes in the chloroplast protein pattern, which in turn would compensate for changes in chloroplast functionality and overall plant performance under abiotic stress. To test this hypothesis, we used a stable isotope-coded protein-labeling technique in conjunction with polyacrylamide gel electrophoresis and liquid chromatography tandem mass spectrometry. We analyzed quantitative and qualitative changes in the chloroplast proteome of isoprene-emitting and non isoprene-emitting poplars. Here we demonstrate that suppression of isoprene synthase by RNA interference resulted in decreased levels of chloroplast proteins involved in photosynthesis and increased levels of histones, ribosomal proteins, and proteins related to metabolism. Overall, our results show that the absence of isoprene triggers a rearrangement of the chloroplast protein profile to minimize the negative stress effects resulting from the absence of isoprene. The present data strongly support the idea that isoprene improves/stabilizes thylakoid membrane structure and interferes with the production of ROS.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Abiotic Stress ; Defense ; Photosynthesis ; Proteomics ; Psi ; Psii ; Volatile Organic Compounds; Photosystem-ii; Oxidative Stress; Serine Hydroxymethyltransferase; Arabidopsis-thaliana; Lipoprotein Particles; Signal-transduction; Lipid-peroxidation; Plastid Proteomics; Carbon Metabolism; Emitting Poplars
ISSN (print) / ISBN 1535-3893
e-ISSN 1535-3907
Quellenangaben Volume: 13, Issue: 4, Pages: 2005-2018 Article Number: , Supplement: ,
Publisher American Chemical Society (ACS)
Publishing Place Washington
Non-patent literature Publications
Reviewing status Peer reviewed