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Comparison of wildtype and gr1 knock-out mutants of Physcomitrella patens using quantitative proteomics

ABSTRACT: (1) While it is known that redox-regulation in chloroplasts is vital for functional photosynthesis, the interplay of different redox-cascades in balancing reactive oxygen species (ROS) with metabolic regulation via thiol switching is still partly unresolved. We investigate the importance of the glutathione reductase isoform maintaining a highly reducing stromal glutathione redox potential (EGSH). (2) Using the model moss Physcomitrella patens, we knocked-out the plastid/mitochondrial GR isoform. We generated a sensor line expressing plastid-targeted redox-sensitive GFP to monitor stromal EGSH in vivo, and compared protein abundances between wildtype (WT) and Δgr1 knock-out mutants by a metabolic labelling approach. (3) On the organelle level, we find that the absence of PpGR1 leads to a shift of stromal EGSH to less reducing values that is not rescued in the light, whereas WT EGSH was clearly responsive to light. On the plant level, growth and photosynthetic performance were decreased with increasing light intensities while ascorbate and zeaxanthin levels were elevated. Proteomics showed an induction of proteins involved in plastid protein repair and degradation. (4) Our results indicate a limited cross-talk between plastid thioredoxin and glutathione redox systems and show that glutathione reductase is necessary for efficient photosynthesis under stress and non-stress conditions.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Physcomitrella Patens Subsp. Patens (moss)

TISSUE(S): Plant Cell, Plant Embryo, Photosynthetic Cell, Protonema

SUBMITTER: Martin Scholz

LAB HEAD: Michael Hippler

PROVIDER: PXD012843 | Pride | 2020-05-06

REPOSITORIES: Pride

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			Action	DRS
	MuellerSchuessele_Table_S2_Proteomics_190219b.xlsx	Xlsx
	RW_16012018_PhyscoWC_WT14N_gr1N15_1hHL_147.raw	Raw
	RW_16012018_PhyscoWC_WT14N_gr1N15_LL_145.raw	Raw
	RW_16012018_PhyscoWC_WT15N_gr1N14_1hHL_148.raw	Raw
	RW_16012018_PhyscoWC_WT15N_gr1N14_LL_146.raw	Raw

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Project description:Tomato (Solanum lycopersicum) is a model species for studying fruit development, wounding, herbivory, and pathogen attack. Despite tomato’s world-wide economic importance and the role of chloroplasts as metabolic hubs and integrators of environmental cues, little is known about the stromal proteome of tomato. Using a high-yielding protocol for chloroplast and stromal protein isolation, MudPIT nano-LC-MS/MS analyses, a robust in-house protein database (the Atlas) for predicting the plastid localization of tomato proteins, and rigorous selection criteria for inclusion/exclusion in the stromal proteome, we identified 1,254 proteins of the tomato stromal proteome. We provide one of the most robust stromal proteomes available to date with empirical evidence for 550 and 105 proteins not previously described for tomato plastids and the Arabidopsis stroma, respectively. The relative abundance of tomato stromal proteins was determined using the exponentially modified protein abundance index (emPAI). Comparison of the abundance of tomato and Arabidopsis stromal proteomes provided evidence for the species-specific nature of stromal protein homeostasis. The manual curation of the tomato stromal proteome classified proteins into ten functional categories resulting in an accessible compendium of tomato chloroplast proteins. After curation, only 88 proteins remained as unknown, uncharacterized or as enzymes with unknown functions. The curation of the tomato stromal proteins also indicated that tomato has a number of paralogous proteins, not present in Arabidopsis, which accumulated to different levels in chloroplasts. As some of these proteins function in key metabolic pathways or in perceiving or transmitting signals critical for plant adaptation to biotic and abiotic stress, these data suggest that tomato may modulate the bidirectional communication between chloroplasts and nuclei in a novel manner. The stromal proteome provides a fertile ground for future mechanistic studies in the field of tomato chloroplast-nuclear signaling and are foundational for our goal of elucidating the dynamics of the stromal proteome controlled by the solanaceous-specific, stromal, and wound-inducible leucine aminopeptidase A of tomato.

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Comparison of wildtype and gr1 knock-out mutants of Physcomitrella patens using quantitative proteomics

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