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Halophilic enzyme activation induced by salts
Halophilic archea (halobacteriae) thrive in hypersaline environments, avoiding osmotic shock by increasing the ion concentration of their cytoplasm by up to 3–6 M. To remain folded and active, their constitutive proteins have evolved towards a biased amino acid composition. High salt concentration a...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3216494/ https://www.ncbi.nlm.nih.gov/pubmed/22355525 http://dx.doi.org/10.1038/srep00006 |
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author | Ortega, Gabriel Laín, Ana Tadeo, Xavier López-Méndez, Blanca Castaño, David Millet, Oscar |
author_facet | Ortega, Gabriel Laín, Ana Tadeo, Xavier López-Méndez, Blanca Castaño, David Millet, Oscar |
author_sort | Ortega, Gabriel |
collection | PubMed |
description | Halophilic archea (halobacteriae) thrive in hypersaline environments, avoiding osmotic shock by increasing the ion concentration of their cytoplasm by up to 3–6 M. To remain folded and active, their constitutive proteins have evolved towards a biased amino acid composition. High salt concentration affects catalytic activity in an enzyme-dependent way and a unified molecular mechanism remains elusive. Here, we have investigated a DNA ligase from Haloferax volcanii (Hv LigN) to show that K(+) triggers catalytic activity by preferentially stabilising a specific conformation in the reaction coordinate. Sodium ions, in turn, do not populate such isoform and the enzyme remains inactive in the presence of this co-solute. Our results show that the halophilic amino acid signature enhances the enzyme's thermodynamic stability, with an indirect effect on its catalytic activity. This model has been successfully applied to reengineer Hv LigN into an enzyme that is catalytically active in the presence of NaCl. |
format | Online Article Text |
id | pubmed-3216494 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-32164942011-12-22 Halophilic enzyme activation induced by salts Ortega, Gabriel Laín, Ana Tadeo, Xavier López-Méndez, Blanca Castaño, David Millet, Oscar Sci Rep Article Halophilic archea (halobacteriae) thrive in hypersaline environments, avoiding osmotic shock by increasing the ion concentration of their cytoplasm by up to 3–6 M. To remain folded and active, their constitutive proteins have evolved towards a biased amino acid composition. High salt concentration affects catalytic activity in an enzyme-dependent way and a unified molecular mechanism remains elusive. Here, we have investigated a DNA ligase from Haloferax volcanii (Hv LigN) to show that K(+) triggers catalytic activity by preferentially stabilising a specific conformation in the reaction coordinate. Sodium ions, in turn, do not populate such isoform and the enzyme remains inactive in the presence of this co-solute. Our results show that the halophilic amino acid signature enhances the enzyme's thermodynamic stability, with an indirect effect on its catalytic activity. This model has been successfully applied to reengineer Hv LigN into an enzyme that is catalytically active in the presence of NaCl. Nature Publishing Group 2011-06-14 /pmc/articles/PMC3216494/ /pubmed/22355525 http://dx.doi.org/10.1038/srep00006 Text en Copyright © 2011, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-ncsa/3.0/ This work is licensed under the Creative Commons Attribution-NonCommercial-Share Alike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/ |
spellingShingle | Article Ortega, Gabriel Laín, Ana Tadeo, Xavier López-Méndez, Blanca Castaño, David Millet, Oscar Halophilic enzyme activation induced by salts |
title | Halophilic enzyme activation induced by salts |
title_full | Halophilic enzyme activation induced by salts |
title_fullStr | Halophilic enzyme activation induced by salts |
title_full_unstemmed | Halophilic enzyme activation induced by salts |
title_short | Halophilic enzyme activation induced by salts |
title_sort | halophilic enzyme activation induced by salts |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3216494/ https://www.ncbi.nlm.nih.gov/pubmed/22355525 http://dx.doi.org/10.1038/srep00006 |
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