DNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.

The oxidative damage hypothesis proposed for the function gain of copper, zinc superoxide dismutase (SOD1) maintains that both mutant and wild-type (WT) SOD1 catalyze reactions with abnormal substrates that damage cellular components critical for viability of the affected cells. However, whether the...

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Autores principales:	Jun Yin, Si Hu, Wei Jiang, Liang Liu, Shemin Lan, Xuegang Song, Changlin Liu
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/83193c58535541049354b47178a0efc3
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spelling	oai:doaj.org-article:83193c58535541049354b47178a0efc32021-11-18T06:35:51ZDNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.1932-620310.1371/journal.pone.0012328https://doaj.org/article/83193c58535541049354b47178a0efc32010-08-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20808835/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The oxidative damage hypothesis proposed for the function gain of copper, zinc superoxide dismutase (SOD1) maintains that both mutant and wild-type (WT) SOD1 catalyze reactions with abnormal substrates that damage cellular components critical for viability of the affected cells. However, whether the oxidative damage of SOD1 is involved in the formation of aggregates rich in SOD1 or not remains elusive. Here, we sought to explore the oxidative aggregation of WT SOD1 exposed to environments containing both ascorbate (Asc) and DNA under neutral conditions. The results showed that the WT SOD1 protein was oxidized in the presence of Asc. The oxidation results in the higher affinity of the modified protein for DNA than that of the unmodified protein. The oxidized SOD1 was observed to be more prone to aggregation than the WT SOD1, and the addition of DNA can significantly accelerate the oxidative aggregation. Moreover, a reasonable relationship can be found between the oxidation, increased hydrophobicity, and aggregation of SOD1 in the presence of DNA. The crucial step in aggregation is neutralization of the positive charges on some SOD1 surfaces by DNA binding. This study might be crucial for understanding molecular forces driving the protein aggregation.Jun YinSi HuWei JiangLiang LiuShemin LanXuegang SongChanglin LiuPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 8, p e12328 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jun Yin Si Hu Wei Jiang Liang Liu Shemin Lan Xuegang Song Changlin Liu DNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.
description	The oxidative damage hypothesis proposed for the function gain of copper, zinc superoxide dismutase (SOD1) maintains that both mutant and wild-type (WT) SOD1 catalyze reactions with abnormal substrates that damage cellular components critical for viability of the affected cells. However, whether the oxidative damage of SOD1 is involved in the formation of aggregates rich in SOD1 or not remains elusive. Here, we sought to explore the oxidative aggregation of WT SOD1 exposed to environments containing both ascorbate (Asc) and DNA under neutral conditions. The results showed that the WT SOD1 protein was oxidized in the presence of Asc. The oxidation results in the higher affinity of the modified protein for DNA than that of the unmodified protein. The oxidized SOD1 was observed to be more prone to aggregation than the WT SOD1, and the addition of DNA can significantly accelerate the oxidative aggregation. Moreover, a reasonable relationship can be found between the oxidation, increased hydrophobicity, and aggregation of SOD1 in the presence of DNA. The crucial step in aggregation is neutralization of the positive charges on some SOD1 surfaces by DNA binding. This study might be crucial for understanding molecular forces driving the protein aggregation.
format	article
author	Jun Yin Si Hu Wei Jiang Liang Liu Shemin Lan Xuegang Song Changlin Liu
author_facet	Jun Yin Si Hu Wei Jiang Liang Liu Shemin Lan Xuegang Song Changlin Liu
author_sort	Jun Yin
title	DNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.
title_short	DNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.
title_full	DNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.
title_fullStr	DNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.
title_full_unstemmed	DNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.
title_sort	dna-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/83193c58535541049354b47178a0efc3
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DNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate.

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