Experimental evidences of the NO action on a recombinant PrxII F from pea plant and its effect preventing the citrate synthase aggregation
| Autor: | Alfonso Lázaro-Payo, Francisca Sevilla, Ana Jiménez, Ana Ortiz-Espín, J. J. Lázaro, María C. Romero-Puertas, Daymi Camejo |
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| Rok vydání: | 2015 |
| Předmět: |
Citrate synthase
Multidisciplinary S-Nitrosylation Biology lcsh:Computer applications to medicine. Medical informatics S-nitrosylation law.invention Transduction (genetics) Biochemistry Peptide mass fingerprinting law Recombinant DNA Posttranslational modification biology.protein Oligomerization lcsh:R858-859.7 PrxII F Research article lcsh:Science (General) Data Article lcsh:Q1-390 |
| Zdroj: | Data in Brief, Vol 3, Iss C, Pp 108-112 (2015) Data in Brief |
| ISSN: | 2352-3409 |
| Popis: | 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 A650nm 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 650nm, respectively. |
| Databáze: | OpenAIRE |
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