Dataset Information

Persulfidation and direct detection of sulfonylation in aging Brain of WT, CSE-/- and MPST-/- mice

ABSTRACT: Cellular homeostasis relies on precise regulation through chemical processes, such as protein posttranslational modifications and physical processes, such as biomolecular condensation. Aging disrupts this balance, increasing susceptibility to diseases and death. However, the mechanisms behind age-related pathogenesis remain unclear. Using chemoproteomic methods to dissect different cysteine posttranslational modifications, we found that age-related changes in cysteine redox homeostasis impact proteins ability to form biomolecular condensates. Age-related increase in sulfenylation and sulfonylation promotes phase separation and through conformational change increases proteins propensity to aggregate. Causing condensates dissolution, protein persulfidation, a protective thiol modification, prevents this. Reduced persulfidation and increased sulfonylation in aging drive abnormal phase separation, leading to shorter life and spontaneous protein aggregation in CSE-/- mice. In this study, we assessed the changes in protein persulfidation levels in brain aging. For this, we used the frontal cortex of 10 weeks, 10 months and 18 months-old WT mice . To unravel the protective role of H2S against ROS, we used the thiol-blocked samples from the persulfidation protocol to directly detect cysteine sulfonylation by mass spectrometry.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Brain, Frontal Lobe

SUBMITTER: Thibaut Vignane

LAB HEAD: Milos Filipovic

PROVIDER: PXD045806 | Pride | 2026-05-23

REPOSITORIES: pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	Eclipse_02845_MmBrain_FP_NBF_LFQ_C145_1_1.raw	Raw
	Eclipse_02845_MmBrain_FP_NBF_LFQ_C145_1_1.raw.refined.mgf	Mgf
	Eclipse_02846_MmBrain_FP_NBF_LFQ_C145_2_1.raw	Raw
	Eclipse_02846_MmBrain_FP_NBF_LFQ_C145_2_1.raw.refined.mgf	Mgf
	Eclipse_02847_MmBrain_FP_NBF_LFQ_C132_1_1.raw	Raw

Items per page:

1 - 5 of 126

Similar Datasets

Project description:Hydrogen sulfide (H2S) is a signaling molecule that regulates essential plant processes, such as autophagy and responses to abiotic stresses. Although there is much information about the processes in which H2S is involved, the mechanism of action of H2S is still unclear. However, the posttranslational modification of cysteine residues, named persulfidation, is the main proposed mechanism. In this study, the role of H2S during drought that allows plant stress adaptation has been analyzed, with the focus on the underlying mechanism. H2S pretreatment before imposing drought on plants significantly improved phenotypic traits and decreased the content of biochemical and molecular drought stress markers. In addition, H2S regulated amino acid metabolism and repressed drought-induced degradation pathways, such as bulk autophagy and protein ubiquitination. The label-free quantitative proteomic analysis of plants growing under control and drought stress identified 887 proteins significantly different persulfidated between both conditions. Bioinformatic analyses revealed that the biological processes most enriched containing the proteins more persulfidated in drought corresponded to cellular response to oxidative stress, and hydrogen peroxide catabolism. In addition, protein degradation, abiotic stress responses, anthocyanin-containing compound biosynthetic process, and flavonoid biosynthesis were highlighted. On the contrary, the most enriched biological process containing proteins with lower levels of persulfidation in drought corresponded to the biosynthetic processes of glucosinolates and chlorophyll. Therefore, our findings emphasize the role of H2S as a promoter of enhanced tolerance to drought, enabling plants to respond more rapidly and efficiently after exposure to drought. Furthermore, the proteomic analysis supports the main role of protein persulfidation as the molecular mechanism of H2S to alleviate ROS accumulation and balance redox homeostasis under drought stress.

Project description:Hydrogen sulfide is an important signaling molecule in plants that regulates essential biological processes through protein persulfidation. Although numerous persulfidated proteins were found to be involved in photorespiration, little was known about sulfide-mediated regulation of photorespiration. Label-free quantitative proteomic analysis has revealed a high impact on the protein persulfidation level when plants grown under non-photorespiratory conditions are transferred to air, with the 97 % of total identified proteins more persulfidated under suppressed photorespiration. A detailed study of the effect of sulfide on important aspects associated with photorespiratory growth conditions has provided insight into the role of sulfide in protecting plants grown under suppressed photorespiration. In these conditions, sulfide amends the metabolic imbalance of carbon/nitrogen and restores ATP levels to concentrations similar to those in air grown conditions. Sulfide also plays an essential role in balancing the significant high level of ROS measured in plants under non-photorespiratory conditions to reach a similar cellular redox state in air-grown plants, through the regulation of antioxidative defenses. Furthermore, sulfide regulates another important characteristic resulting from suppression of photorespiration, such as the stomata closure, to decrease the high guard cell ROS levels and inducing the stomata aperture. In this way, sulfide signals the movement of the CO2-dependent stomata to achieve a scenario similar to that of plants growing under normal air conditions, in the opposite direction of the already established ABA-dependent movement of the stomata. Therefore, our findings suggest that the high persulfidation level under suppressed photorespiration reveals an essential role of sulfide signaling under these conditions, and with respect to stomatal movement, the outcome of this signaling is dependent on the growth/stress condition under study.

Dataset Information

Persulfidation and direct detection of sulfonylation in aging Brain of WT, CSE-/- and MPST-/- mice

Dataset's files

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets