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The Archaeal Small Heat Shock Protein Hsp17.6 Protects Proteins from Oxidative Inactivation

Small heat shock proteins (sHsps) are widely distributed among various types of organisms and function in preventing the irreversible aggregation of thermal denaturing proteins. Here, we report that Hsp17.6 from Methanolobus psychrophilus exhibited protection of proteins from oxidation inactivation....

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Autores principales: Ma, Pengfei, Li, Jie, Qi, Lei, Dong, Xiuzhu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7961418/
https://www.ncbi.nlm.nih.gov/pubmed/33806708
http://dx.doi.org/10.3390/ijms22052591
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author Ma, Pengfei
Li, Jie
Qi, Lei
Dong, Xiuzhu
author_facet Ma, Pengfei
Li, Jie
Qi, Lei
Dong, Xiuzhu
author_sort Ma, Pengfei
collection PubMed
description Small heat shock proteins (sHsps) are widely distributed among various types of organisms and function in preventing the irreversible aggregation of thermal denaturing proteins. Here, we report that Hsp17.6 from Methanolobus psychrophilus exhibited protection of proteins from oxidation inactivation. The overexpression of Hsp17.6 in Escherichia coli markedly increased the stationary phase cell density and survivability in HClO and H(2)O(2). Treatments with 0.2 mM HClO or 10 mM H(2)O(2) reduced malate dehydrogenase (MDH) activity to 57% and 77%, whereas the addition of Hsp17.6 recovered the activity to 70–90% and 86–100%, respectively. A similar effect for superoxide dismutase oxidation was determined for Hsp17.6. Non-reducing sodium dodecyl sulfate polyacrylamide gel electrophoresis assays determined that the Hsp17.6 addition decreased H(2)O(2)-caused disulfide-linking protein contents and HClO-induced degradation of MDH; meanwhile, Hsp17.6 protein appeared to be oxidized with increased molecular weights. Mass spectrometry identified oxygen atoms introduced into the larger Hsp17.6 molecules, mainly at the aspartate and methionine residues. Substitution of some aspartate residues reduced Hsp17.6 in alleviating H(2)O(2)- and HClO-caused MDH inactivation and in enhancing the E. coli survivability in H(2)O(2) and HClO, suggesting that the archaeal Hsp17.6 oxidation protection might depend on an “oxidant sink” effect, i.e., to consume the oxidants in environments via aspartate oxidation.
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spelling pubmed-79614182021-03-17 The Archaeal Small Heat Shock Protein Hsp17.6 Protects Proteins from Oxidative Inactivation Ma, Pengfei Li, Jie Qi, Lei Dong, Xiuzhu Int J Mol Sci Article Small heat shock proteins (sHsps) are widely distributed among various types of organisms and function in preventing the irreversible aggregation of thermal denaturing proteins. Here, we report that Hsp17.6 from Methanolobus psychrophilus exhibited protection of proteins from oxidation inactivation. The overexpression of Hsp17.6 in Escherichia coli markedly increased the stationary phase cell density and survivability in HClO and H(2)O(2). Treatments with 0.2 mM HClO or 10 mM H(2)O(2) reduced malate dehydrogenase (MDH) activity to 57% and 77%, whereas the addition of Hsp17.6 recovered the activity to 70–90% and 86–100%, respectively. A similar effect for superoxide dismutase oxidation was determined for Hsp17.6. Non-reducing sodium dodecyl sulfate polyacrylamide gel electrophoresis assays determined that the Hsp17.6 addition decreased H(2)O(2)-caused disulfide-linking protein contents and HClO-induced degradation of MDH; meanwhile, Hsp17.6 protein appeared to be oxidized with increased molecular weights. Mass spectrometry identified oxygen atoms introduced into the larger Hsp17.6 molecules, mainly at the aspartate and methionine residues. Substitution of some aspartate residues reduced Hsp17.6 in alleviating H(2)O(2)- and HClO-caused MDH inactivation and in enhancing the E. coli survivability in H(2)O(2) and HClO, suggesting that the archaeal Hsp17.6 oxidation protection might depend on an “oxidant sink” effect, i.e., to consume the oxidants in environments via aspartate oxidation. MDPI 2021-03-04 /pmc/articles/PMC7961418/ /pubmed/33806708 http://dx.doi.org/10.3390/ijms22052591 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Ma, Pengfei
Li, Jie
Qi, Lei
Dong, Xiuzhu
The Archaeal Small Heat Shock Protein Hsp17.6 Protects Proteins from Oxidative Inactivation
title The Archaeal Small Heat Shock Protein Hsp17.6 Protects Proteins from Oxidative Inactivation
title_full The Archaeal Small Heat Shock Protein Hsp17.6 Protects Proteins from Oxidative Inactivation
title_fullStr The Archaeal Small Heat Shock Protein Hsp17.6 Protects Proteins from Oxidative Inactivation
title_full_unstemmed The Archaeal Small Heat Shock Protein Hsp17.6 Protects Proteins from Oxidative Inactivation
title_short The Archaeal Small Heat Shock Protein Hsp17.6 Protects Proteins from Oxidative Inactivation
title_sort archaeal small heat shock protein hsp17.6 protects proteins from oxidative inactivation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7961418/
https://www.ncbi.nlm.nih.gov/pubmed/33806708
http://dx.doi.org/10.3390/ijms22052591
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