Proteomics

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


ABSTRACT: Plants must cope with a variety of different stressors during their life cycle and their adaptations to these environmental influences involves all cellular organelles. Among them, comparatively little is known about the contribution of cytosolic lipid droplets (LDs) and their core 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 leaves after pathogen infections with Botrytis cinerea and Pseudomonas syringae, and heat stress. Analyses were carried out in wild-type plants and the oil-rich double mutant tgd1-1 sdp1-4 that allowed an allied study of the LD proteome in stressed leaves. Using liquid chromatography-tandem mass spectrometry-based methods, we show that a hyperaccumulation of the primary LD core component triacylglycerol is a general response to stress and that acyl chains are remodeled during cellular adaptation. Likewise, comparative analysis of the LD protein composition in stress-treated leaves highlighted the remodeling of the LD proteome as part of the general stress response. We further identified two new LD-associated proteins whose localization to LDs in leaves was confirmed by confocal microscopy of fluorescent protein fusions. Taken together, these and other results highlight LDs as dynamic contributors to the cellular adaptation processes that underlie how plants respond to environmental stress.

INSTRUMENT(S): LTQ Orbitrap Velos, Q Exactive HF

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Leaf

SUBMITTER: Till Ischebeck  

LAB HEAD: Till Ischebeck

PROVIDER: PXD045596 | Pride | 2025-03-21

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
MaxQuant_1.6.17.0.zip Other
Metadatafile.pdf Pdf
PS_Q_10.raw Raw
PS_Q_11.raw Raw
PS_Q_12.raw Raw
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