Abstract
S-nitrosylation is emerging as a key post-translational protein modification for the transduction of NO as a signaling molecule in plants. This data article supports the research article entitled “Functional and structural changes in plant mitochondrial PrxII F caused by NO” [1]. To identify the Cys residues of the recombinant PrxII F modified after the treatment with S-nitrosylating agents we performed the LC ESI–QTOF tandem MS and MALDI peptide mass fingerprinting analysis. Change in A650 nm was monitored to estimate the thermal aggregation of citrate synthase in the presence S-nitrosylated PrxII F. The effect of the temperature on the oligomerization pattern and aggregation of PrxII F was analysed by SDS-PAGE and changes in absorbance at 650 nm, respectively.
Highlights
S-nitrosylation is emerging as a key post-translational protein modification for the transduction of NO as a signaling molecule in plants
To identify the Cys residues of the recombinant PrxII F modified after the treatment with S-nitrosylating agents we performed the LC ESI–QTOF tandem MS and MALDI peptide mass fingerprinting analysis
PsPrxII F treated with 5 mM GSNO was run in SDS-PAGE and the visualized bands were analysed by TOF QTOF mass spectrometry (Fig. 1)
Summary
Daymi Camejo a, Ana Ortiz-Espín a, Juan J. Romero-Puertas b, Alfonso Lázaro-Payo b, Francisca Sevilla a, Ana Jiménez a,n a CEBAS-CSIC, Department of Stress Biology and Plant Pathology, E-30100 Murcia, Spain b EEZ-CSIC, Department of Biochemistry, Cellular and Molecular Biology of Plants, E-18080 Granada, Spain article info. S-nitrosylation is emerging as a key post-translational protein modification for the transduction of NO as a signaling molecule in plants. This data article supports the research article entitled “Functional and structural changes in plant mitochondrial PrxII F caused by NO” [1].
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