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Experimental evidences of the NO action on a recombinant PrxII F from pea plant and its effect preventing the citrate synthase aggregation

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...

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Autores principales: Camejo, Daymi, Ortiz-Espín, Ana, Lázaro, Juan J., Romero-Puertas, María C., Lázaro-Payo, Alfonso, Sevilla, Francisca, Jiménez, Ana
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4510073/
https://www.ncbi.nlm.nih.gov/pubmed/26217728
http://dx.doi.org/10.1016/j.dib.2015.02.009
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author Camejo, Daymi
Ortiz-Espín, Ana
Lázaro, Juan J.
Romero-Puertas, María C.
Lázaro-Payo, Alfonso
Sevilla, Francisca
Jiménez, Ana
author_facet Camejo, Daymi
Ortiz-Espín, Ana
Lázaro, Juan J.
Romero-Puertas, María C.
Lázaro-Payo, Alfonso
Sevilla, Francisca
Jiménez, Ana
author_sort Camejo, Daymi
collection PubMed
description 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 A(650 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.
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spelling pubmed-45100732015-07-27 Experimental evidences of the NO action on a recombinant PrxII F from pea plant and its effect preventing the citrate synthase aggregation Camejo, Daymi Ortiz-Espín, Ana Lázaro, Juan J. Romero-Puertas, María C. Lázaro-Payo, Alfonso Sevilla, Francisca Jiménez, Ana Data Brief Data Article 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 A(650 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. Elsevier 2015-02-26 /pmc/articles/PMC4510073/ /pubmed/26217728 http://dx.doi.org/10.1016/j.dib.2015.02.009 Text en © 2015 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Data Article
Camejo, Daymi
Ortiz-Espín, Ana
Lázaro, Juan J.
Romero-Puertas, María C.
Lázaro-Payo, Alfonso
Sevilla, Francisca
Jiménez, Ana
Experimental evidences of the NO action on a recombinant PrxII F from pea plant and its effect preventing the citrate synthase aggregation
title Experimental evidences of the NO action on a recombinant PrxII F from pea plant and its effect preventing the citrate synthase aggregation
title_full Experimental evidences of the NO action on a recombinant PrxII F from pea plant and its effect preventing the citrate synthase aggregation
title_fullStr Experimental evidences of the NO action on a recombinant PrxII F from pea plant and its effect preventing the citrate synthase aggregation
title_full_unstemmed Experimental evidences of the NO action on a recombinant PrxII F from pea plant and its effect preventing the citrate synthase aggregation
title_short Experimental evidences of the NO action on a recombinant PrxII F from pea plant and its effect preventing the citrate synthase aggregation
title_sort experimental evidences of the no action on a recombinant prxii f from pea plant and its effect preventing the citrate synthase aggregation
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4510073/
https://www.ncbi.nlm.nih.gov/pubmed/26217728
http://dx.doi.org/10.1016/j.dib.2015.02.009
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