Plasticity of the Arabidopsis leaf lipidome and proteome in response to pathogen infection and heat stress

Author:

Scholz Patricia1ORCID,Doner Nathan M2ORCID,Gutbrod Katharina3ORCID,Herrfurth Cornelia14ORCID,Niemeyer Philipp W1ORCID,Lim Magdiel S S5ORCID,Blersch Katharina F5ORCID,Schmitt Kerstin6ORCID,Valerius Oliver6ORCID,Shanklin John7ORCID,Feussner Ivo14ORCID,Dörmann Peter3ORCID,Braus Gerhard H46ORCID,Mullen Robert T2ORCID,Ischebeck Till145ORCID

Affiliation:

1. Albrecht-von-Haller-Institute for Plant Sciences, Department of Plant Biochemistry, University of Goettingen , Goettingen 37077 , Germany

2. Department of Molecular and Cellular Biology, University of Guelph , Guelph, ON N1G 2W1 , Canada

3. Institute of Molecular Physiology and Biotechnology of Plants (IMBIO), University of Bonn , Bonn 53115 , Germany

4. Goettingen Center for Molecular Biosciences (GZMB), University of Goettingen , Goettingen 37077 , Germany

5. Green Biotechnology, Institute of Plant Biology and Biotechnology (IBBP), University of Münster , Münster 48143 , Germany

6. Institute for Microbiology and Genetics, Service Unit LCMS Protein Analytics Department for Molecular Microbiology and Genetics, University of Goettingen , Goettingen 37077 , Germany

7. Department of Biology, Brookhaven National Laboratory , Upton, NY 11973 , USA

Abstract

Abstract Plants must cope with a variety of stressors during their life cycle, and the adaptive responses to these environmental cues involve all cellular organelles. Among them, comparatively little is known about the contribution of cytosolic lipid droplets (LDs) and their core set of neutral lipids and associated surface proteins to the rewiring of cellular processes in response to stress. Here, we analyzed the changes that occur in the lipidome and proteome of Arabidopsis (Arabidopsis thaliana) leaves after pathogen infection with Botrytis cinerea or Pseudomonas syringae, or after heat stress. Analyses were carried out in wild-type plants and the oil-rich double mutant trigalactosyldiacylglycerol1-1 sugar dependent 1-4 (tgd1-1 sdp1-4) that allowed for an allied study of the LD proteome in stressed leaves. Using liquid chromatography-tandem mass spectrometry-based methods, we showed that a hyperaccumulation of the primary LD core lipid TAG is a general response to stress and that acyl chain and sterol composition are remodeled during cellular adaptation. Likewise, comparative analysis of the LD protein composition in stress-treated leaves highlighted the plasticity of the LD proteome as part of the general stress response. We further identified at least two additional LD-associated proteins, whose localization to LDs in leaves was confirmed by confocal microscopy of fluorescent protein fusions. Taken together, these results highlight LDs as dynamic contributors to the cellular adaptation processes that underlie how plants respond to environmental stress.

Funder

German Research Foundation

U.S. Department of Energy

Office of Science

BES-Physical Biosciences Program

Natural Sciences and Engineering Research Council of Canada

Ontario Graduate Scholarship

Publisher

Oxford University Press (OUP)

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