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Growth-Dependent Catalase Localization in Exiguobacterium oxidotolerans T-2-2(T) Reflected by Catalase Activity of Cells

A psychrotolerant and H(2)O(2)-resistant bacterium, Exiguobacterium oxidotolerans T-2-2(T), exhibits extraordinary H(2)O(2) resistance and produces catalase not only intracellularly but also extracellularly. The intracellular and extracellular catalases exhibited the same enzymatic characteristics,...

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Autores principales: Hanaoka, Yoshiko, Takebe, Fumihiko, Nodasaka, Yoshinobu, Hara, Isao, Matsuyama, Hidetoshi, Yumoto, Isao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3800074/
https://www.ncbi.nlm.nih.gov/pubmed/24204687
http://dx.doi.org/10.1371/journal.pone.0076862
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author Hanaoka, Yoshiko
Takebe, Fumihiko
Nodasaka, Yoshinobu
Hara, Isao
Matsuyama, Hidetoshi
Yumoto, Isao
author_facet Hanaoka, Yoshiko
Takebe, Fumihiko
Nodasaka, Yoshinobu
Hara, Isao
Matsuyama, Hidetoshi
Yumoto, Isao
author_sort Hanaoka, Yoshiko
collection PubMed
description A psychrotolerant and H(2)O(2)-resistant bacterium, Exiguobacterium oxidotolerans T-2-2(T), exhibits extraordinary H(2)O(2) resistance and produces catalase not only intracellularly but also extracellularly. The intracellular and extracellular catalases exhibited the same enzymatic characteristics, that is, they exhibited the temperature-dependent activity characteristic of a cold-adapted enzyme, their heat stabilities were similar to those of mesophilic enzymes and very high catalytic intensity. In addition, catalase gene analysis indicated that the bacterium possessed the sole clade 1 catalase gene corresponding to intracellular catalase. Hence, intracellular catalase is secreted into the extracellular space. In addition to intracellular and extracellular catalases, the inner circumference of the cells showed the localization of catalase in the mid-stationary growth phase, which was observed by immunoelectron microscopy using an antibody against the intracellular catalase of the strain. The cells demonstrated higher catalase activity in the mid-stationary growth phase than in the exponential growth phase. The catalase localized in the inner circumference can be dissociated by treatment with Tween 60. Thus, the localized catalase is not tightly bound to the inner circumference of the cells and may play a role in the oxidative defense of the cells under low metabolic state.
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spelling pubmed-38000742013-11-07 Growth-Dependent Catalase Localization in Exiguobacterium oxidotolerans T-2-2(T) Reflected by Catalase Activity of Cells Hanaoka, Yoshiko Takebe, Fumihiko Nodasaka, Yoshinobu Hara, Isao Matsuyama, Hidetoshi Yumoto, Isao PLoS One Research Article A psychrotolerant and H(2)O(2)-resistant bacterium, Exiguobacterium oxidotolerans T-2-2(T), exhibits extraordinary H(2)O(2) resistance and produces catalase not only intracellularly but also extracellularly. The intracellular and extracellular catalases exhibited the same enzymatic characteristics, that is, they exhibited the temperature-dependent activity characteristic of a cold-adapted enzyme, their heat stabilities were similar to those of mesophilic enzymes and very high catalytic intensity. In addition, catalase gene analysis indicated that the bacterium possessed the sole clade 1 catalase gene corresponding to intracellular catalase. Hence, intracellular catalase is secreted into the extracellular space. In addition to intracellular and extracellular catalases, the inner circumference of the cells showed the localization of catalase in the mid-stationary growth phase, which was observed by immunoelectron microscopy using an antibody against the intracellular catalase of the strain. The cells demonstrated higher catalase activity in the mid-stationary growth phase than in the exponential growth phase. The catalase localized in the inner circumference can be dissociated by treatment with Tween 60. Thus, the localized catalase is not tightly bound to the inner circumference of the cells and may play a role in the oxidative defense of the cells under low metabolic state. Public Library of Science 2013-10-18 /pmc/articles/PMC3800074/ /pubmed/24204687 http://dx.doi.org/10.1371/journal.pone.0076862 Text en © 2013 Hanaoka et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Hanaoka, Yoshiko
Takebe, Fumihiko
Nodasaka, Yoshinobu
Hara, Isao
Matsuyama, Hidetoshi
Yumoto, Isao
Growth-Dependent Catalase Localization in Exiguobacterium oxidotolerans T-2-2(T) Reflected by Catalase Activity of Cells
title Growth-Dependent Catalase Localization in Exiguobacterium oxidotolerans T-2-2(T) Reflected by Catalase Activity of Cells
title_full Growth-Dependent Catalase Localization in Exiguobacterium oxidotolerans T-2-2(T) Reflected by Catalase Activity of Cells
title_fullStr Growth-Dependent Catalase Localization in Exiguobacterium oxidotolerans T-2-2(T) Reflected by Catalase Activity of Cells
title_full_unstemmed Growth-Dependent Catalase Localization in Exiguobacterium oxidotolerans T-2-2(T) Reflected by Catalase Activity of Cells
title_short Growth-Dependent Catalase Localization in Exiguobacterium oxidotolerans T-2-2(T) Reflected by Catalase Activity of Cells
title_sort growth-dependent catalase localization in exiguobacterium oxidotolerans t-2-2(t) reflected by catalase activity of cells
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3800074/
https://www.ncbi.nlm.nih.gov/pubmed/24204687
http://dx.doi.org/10.1371/journal.pone.0076862
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