Dataset Information

Daylily proteomics LC-MSMS

ABSTRACT: The study was aimed at the identification and quantification of the protein components of the pollen grains in parallel with the distal stigmatic tissues of daylily. Proteins were identified and quantified using iTRAQ 4-plex labeling on an orbitrap fusion Mass spectrometer. 128 differentially expressed proteins were retained for further analysis.

INSTRUMENT(S):

ORGANISM(S): Asparagales

TISSUE(S): Stigma, Pollen

SUBMITTER: sylvie Bourassa

LAB HEAD: Sylvie Bourassa

PROVIDER: PXD005007 | Pride | 2022-03-04

REPOSITORIES: Pride

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Source:

			Action	DRS
	iTRAQ133.tgz	Other
	iTRAQ133_TremblayR_AfterTRaining.msf	Msf

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Project description:Heat stress is a major cause for yield loss in many crops, including vegetable crops. Even short waves of high temperature, becoming more frequent during recent years, can be detrimental. Pollen development is most heat-sensitive, being the main cause for reduced productivity under heat-stress across a wide range of crops. The molecular mechanisms involved in pollen heat-stress response and thermotolerance are however not fully understood. Recently, we have demonstrated that ethylene, a gaseous plant hormone, plays a role in tomato (Solanum lycopersicum) pollen thermotolerance. These results were substantiated in the current work showing that increasing ethylene levels by using an ethylene-releasing substance, ethephon, prior to heat-stress exposure, increased pollen quality. A proteomic approach was undertaken, to unravel the mechanisms underlying pollen heat-stress response and ethylene-mediated pollen thermotolerance in developing pollen grains. Proteins were extracted and analyzed by means of a gel LC-MS fractionation protocol, and a total of 1355 proteins were identified. A dataset of 721 proteins, detected in three biological replicates of at least one of the applied treatments, was used for all analyses. Quantitative analysis was performed based on peptide count. The analysis revealed that heat-stress affected the developmental program of pollen, including protein homeostasis (components of the translational and degradation machinery), carbohydrate and energy metabolism. Ethephon-pretreatment shifted the heat-stressed pollen proteome closer to the proteome under non-stressful conditions, namely, by showing higher abundance of proteins involved in protein synthesis, degradation, tricarboxylic acid cycle and RNA regulation. Furthermore, up-regulation of protective mechanisms against oxidative stress was observed following ethephon-treatment (including higher abundance of glutathione-disulfide reductase, glutaredoxin and protein disulfide isomerase). Taken together, the findings identified systemic and fundamental components of pollen thermotolerance, and serve as a valuable quantitative protein database for further research.

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Daylily proteomics LC-MSMS

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