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Genetic manipulation of isoprene emissions in poplar plants remodels the chloroplast proteome.
J. Proteome Res. 13, 2005-2018 (2014)
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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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
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
Zeitschrift
Journal of Proteome Research
Quellenangaben
Band: 13,
Heft: 4,
Seiten: 2005-2018
Verlag
American Chemical Society (ACS)
Verlagsort
Washington
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed