Dataset Information

Carbonylation proteome of rice embryo

ABSTRACT: Using affinity chromatography to enrich carbonylated proteins from rice embryos germinated for 0, 24, 48, 72 h. Sequential window acquisition of all therotical spectra (SWATH) technology was used to quantify carbonylated proteins. Mass spectra data was searched to discover carbonylated peptides and their corresponding proteins.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Oryza Sativa (rice)

TISSUE(S): Plant Cell, Embryo

SUBMITTER: Zhang Hui

LAB HEAD: Pingfang Yang

PROVIDER: PXD001429 | Pride | 2016-02-01

REPOSITORIES: Pride

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Publications

Analysis of dynamic protein carbonylation in rice embryo during germination through AP-SWATH.

Zhang Hui H He Dongli D Yu Jianlan J Li Ming M Damaris Rebecca Njeri RN Gupta Ravi R Kim Sun Tae ST Yang Pingfang P

Proteomics 20160301 6

Seed germination is an important aspect of the plant life cycle, during which, reactive oxygen species (ROS) accumulate. The accumulation of ROS results in an increase in protein oxidation of which carbonylation is the most canonical one. However, there is insufficient information concerning protein oxidation, especially carbonylation and its contribution to seed germination. In this study, biotin hydrazide labeled chromatography combined with sequential window acquisition of all theoretical fra ...[more]

PMID: 26801057

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Project description:Exposure to Paraquat and RNA interference knockdown of mitochondrial superoxide dismutase (Sod2) are known to result in significant lifespan reduction, locomotor dysfunction, and mitochondrial degeneration in Drosophila melanogaster. Both perturbations increase the flux of superoxide, a progenitor reactive oxygen species, but the molecular underpinnings of the resulting phenotypes are poorly understood. Improved understanding of such processes could lead to advances in the treatment of numerous age-related disorders. Superoxide toxicity can act through protein carbonylation. Analysis of carbonylated proteins is attractive since reactive carbonyl groups are not present in the twenty canonical amino acids and are amenable to labeling and enrichment strategies. Here, carbonylated proteins were labeled with biotin hydrazide and enriched on streptavidin-coated beads. On-bead digestion was used to release carbonylated protein peptides, with relative abundance ratios versus controls obtained using the iTRAQ mass spectrometry-based proteomics approach. While Paraquat exposure and Sod2 knockdown have similar phenotypes, differences in protein carbonylation were anticipated because Paraquat exposure was expected to increase the concentration of superoxide throughout the cell while Sod2 knockdown was only expected to raise the concentration of superoxide in the mitochondrial matrix. Paraquat exposure resulted in widespread increases in carbonylated protein relative abundance: the median Paraquat-exposed to control carbonylated protein relative abundance ratio was 1.53. For Sod2 knockdown, in contrast, the median carbonylated protein relative abundance ratios were 1.13 versus the RNA interference driver control and 1.05 versus the RNA interference transgene control. However, some proteins did show large increases in carbonylated protein relative abundance on Sod2 knockdown, most notably cytochrome c oxidase subunit Vb, possibly providing some indication of the molecular basis of the Sod2-knockdown phenotype.

Dataset Information

Carbonylation proteome of rice embryo

Publications

Analysis of dynamic protein carbonylation in rice embryo during germination through AP-SWATH.

Similar Datasets

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