The Richness and Diversity of Catalases in Bacteria

Catalases play a key role in the defense against oxidative stress in bacteria by catalyzing the decomposition of H2O2. In addition, catalases are also involved in multiple cellular processes, such as cell development and differentiation, as well as metabolite production. However, little is known abo...

Full description

Bibliographic Details
Main Authors: Fang Yuan, Shouliang Yin, Yang Xu, Lijun Xiang, Haiyan Wang, Zilong Li, Keqiang Fan, Guohui Pan
Format: Article
Language:English
Published: Frontiers Media S.A. 2021-03-01
Series:Frontiers in Microbiology
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fmicb.2021.645477/full
_version_ 1818368921053429760
author Fang Yuan
Fang Yuan
Shouliang Yin
Shouliang Yin
Yang Xu
Lijun Xiang
Haiyan Wang
Zilong Li
Keqiang Fan
Guohui Pan
Guohui Pan
author_facet Fang Yuan
Fang Yuan
Shouliang Yin
Shouliang Yin
Yang Xu
Lijun Xiang
Haiyan Wang
Zilong Li
Keqiang Fan
Guohui Pan
Guohui Pan
author_sort Fang Yuan
collection DOAJ
description Catalases play a key role in the defense against oxidative stress in bacteria by catalyzing the decomposition of H2O2. In addition, catalases are also involved in multiple cellular processes, such as cell development and differentiation, as well as metabolite production. However, little is known about the abundance, diversity, and distribution of catalases in bacteria. In this study, we systematically surveyed and classified the homologs of three catalase families from 2,634 bacterial genomes. It was found that both of the typical catalase and Mn-catalase families could be divided into distinct groups, while the catalase-peroxidase homologs formed a tight family. The typical catalases are rich in all the analyzed bacterial phyla except Chlorobi, in which the catalase-peroxidases are dominant. Catalase-peroxidases are rich in many phyla, but lacking in Deinococcus-Thermus, Spirochetes, and Firmicutes. Mn-catalases are found mainly in Firmicutes and Deinococcus-Thermus, but are rare in many other phyla. Given the fact that catalases were reported to be involved in secondary metabolite biosynthesis in several Streptomyces strains, the distribution of catalases in the genus Streptomyces was given more attention herein. On average, there are 2.99 typical catalases and 0.99 catalase-peroxidases in each Streptomyces genome, while no Mn-catalases were identified. To understand detailed properties of catalases in Streptomyces, we characterized all the five typical catalases from S. rimosus ATCC 10970, the oxytetracycline-producing strain. The five catalases showed typical catalase activity, but possessed different catalytic properties. Our findings contribute to the more detailed classification of catalases and facilitate further studies about their physiological roles in secondary metabolite biosynthesis and other cellular processes, which might facilitate the yield improvement of valuable secondary metabolites in engineered bacteria.
first_indexed 2024-12-13T23:15:37Z
format Article
id doaj.art-2bc05c4f0d75477fba88f644301aa14c
institution Directory Open Access Journal
issn 1664-302X
language English
last_indexed 2024-12-13T23:15:37Z
publishDate 2021-03-01
publisher Frontiers Media S.A.
record_format Article
series Frontiers in Microbiology
spelling doaj.art-2bc05c4f0d75477fba88f644301aa14c2022-12-21T23:27:56ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2021-03-011210.3389/fmicb.2021.645477645477The Richness and Diversity of Catalases in BacteriaFang Yuan0Fang Yuan1Shouliang Yin2Shouliang Yin3Yang Xu4Lijun Xiang5Haiyan Wang6Zilong Li7Keqiang Fan8Guohui Pan9Guohui Pan10State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, ChinaUniversity of Chinese Academy of Sciences, Beijing, ChinaState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, ChinaSchool of Life Sciences, North China University of Science and Technology, Tangshan, ChinaState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, ChinaState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, ChinaState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, ChinaState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, ChinaState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, ChinaState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, ChinaUniversity of Chinese Academy of Sciences, Beijing, ChinaCatalases play a key role in the defense against oxidative stress in bacteria by catalyzing the decomposition of H2O2. In addition, catalases are also involved in multiple cellular processes, such as cell development and differentiation, as well as metabolite production. However, little is known about the abundance, diversity, and distribution of catalases in bacteria. In this study, we systematically surveyed and classified the homologs of three catalase families from 2,634 bacterial genomes. It was found that both of the typical catalase and Mn-catalase families could be divided into distinct groups, while the catalase-peroxidase homologs formed a tight family. The typical catalases are rich in all the analyzed bacterial phyla except Chlorobi, in which the catalase-peroxidases are dominant. Catalase-peroxidases are rich in many phyla, but lacking in Deinococcus-Thermus, Spirochetes, and Firmicutes. Mn-catalases are found mainly in Firmicutes and Deinococcus-Thermus, but are rare in many other phyla. Given the fact that catalases were reported to be involved in secondary metabolite biosynthesis in several Streptomyces strains, the distribution of catalases in the genus Streptomyces was given more attention herein. On average, there are 2.99 typical catalases and 0.99 catalase-peroxidases in each Streptomyces genome, while no Mn-catalases were identified. To understand detailed properties of catalases in Streptomyces, we characterized all the five typical catalases from S. rimosus ATCC 10970, the oxytetracycline-producing strain. The five catalases showed typical catalase activity, but possessed different catalytic properties. Our findings contribute to the more detailed classification of catalases and facilitate further studies about their physiological roles in secondary metabolite biosynthesis and other cellular processes, which might facilitate the yield improvement of valuable secondary metabolites in engineered bacteria.https://www.frontiersin.org/articles/10.3389/fmicb.2021.645477/fullcatalasehydrogen peroxidemonofunctional catalasecatalase-peroxidasemanganese-containing catalasebacteria
spellingShingle Fang Yuan
Fang Yuan
Shouliang Yin
Shouliang Yin
Yang Xu
Lijun Xiang
Haiyan Wang
Zilong Li
Keqiang Fan
Guohui Pan
Guohui Pan
The Richness and Diversity of Catalases in Bacteria
Frontiers in Microbiology
catalase
hydrogen peroxide
monofunctional catalase
catalase-peroxidase
manganese-containing catalase
bacteria
title The Richness and Diversity of Catalases in Bacteria
title_full The Richness and Diversity of Catalases in Bacteria
title_fullStr The Richness and Diversity of Catalases in Bacteria
title_full_unstemmed The Richness and Diversity of Catalases in Bacteria
title_short The Richness and Diversity of Catalases in Bacteria
title_sort richness and diversity of catalases in bacteria
topic catalase
hydrogen peroxide
monofunctional catalase
catalase-peroxidase
manganese-containing catalase
bacteria
url https://www.frontiersin.org/articles/10.3389/fmicb.2021.645477/full
work_keys_str_mv AT fangyuan therichnessanddiversityofcatalasesinbacteria
AT fangyuan therichnessanddiversityofcatalasesinbacteria
AT shouliangyin therichnessanddiversityofcatalasesinbacteria
AT shouliangyin therichnessanddiversityofcatalasesinbacteria
AT yangxu therichnessanddiversityofcatalasesinbacteria
AT lijunxiang therichnessanddiversityofcatalasesinbacteria
AT haiyanwang therichnessanddiversityofcatalasesinbacteria
AT zilongli therichnessanddiversityofcatalasesinbacteria
AT keqiangfan therichnessanddiversityofcatalasesinbacteria
AT guohuipan therichnessanddiversityofcatalasesinbacteria
AT guohuipan therichnessanddiversityofcatalasesinbacteria
AT fangyuan richnessanddiversityofcatalasesinbacteria
AT fangyuan richnessanddiversityofcatalasesinbacteria
AT shouliangyin richnessanddiversityofcatalasesinbacteria
AT shouliangyin richnessanddiversityofcatalasesinbacteria
AT yangxu richnessanddiversityofcatalasesinbacteria
AT lijunxiang richnessanddiversityofcatalasesinbacteria
AT haiyanwang richnessanddiversityofcatalasesinbacteria
AT zilongli richnessanddiversityofcatalasesinbacteria
AT keqiangfan richnessanddiversityofcatalasesinbacteria
AT guohuipan richnessanddiversityofcatalasesinbacteria
AT guohuipan richnessanddiversityofcatalasesinbacteria