» Articles » PMID: 31191509

Arsenite Oxidation by a Newly Isolated Betaproteobacterium Possessing Genes and Diversity of the Gene Cluster in Bacterial Genomes

Overview
Journal Front Microbiol
Specialty Microbiology
Date 2019 Jun 14
PMID 31191509
Citations 3
Authors
Affiliations
Soon will be listed here.
Abstract

Microbes play essential roles in arsenic transformation in the environment. Microbial arsenite oxidation is catalyzed by either of two distantly related arsenite oxidases, referred to as AIO and ARX. The genes encoding ARX and its regulatory proteins were originally defined in the genomes of gammaproteobacteria isolated from an alkaline soda lake. The gene cluster has been identified in a limited number of bacteria, predominantly in gammaproteobacteria isolated from lakes characterized by high pH and high salinity. In the present study, a novel arsenite-oxidizing betaproteobacterium, strain M52, was isolated from a hot spring microbial mat. The strain oxidized arsenite under both microaerophilic and nitrate-reducing conditions at nearly neutral pH. Genome analysis revealed that the strain possesses the gene cluster in its genome and lacks genes encoding AIO. Inspection of the bacterial genomes available in the GenBank database revealed that the presence of this gene cluster is restricted to genomes of , mainly in the classes and . In these genomes, the structure of the gene cluster was generally well-conserved, but genes for regulatory proteins were lacking in genomes of strains belonging to a specific lineage. Phylogenetic analysis suggested that ARX encoded in the genomes can be divided into three groups, and strain M52 belongs to a group specific for organisms living in low-salt environments. The ArxA protein encoded in the genome of strain M52 was characterized by the presence of a long insertion, which was specifically observed in the same group of ARX. In clone library analyses with a newly designed primer pair, a diverse ArxA sequence with a long insertion was detected in samples of lake water and hot spring microbial mat, characterized by low salinity and a nearly neutral pH. Among the isolated bacterial strains whose arsenite oxidation has been demonstrated, strain M52 is the first betaproteobacterium that possesses the genes, the first strain encoding ARX of the group specific for low-salt environments, and the first organism possessing the gene encoding ArxA with a long insertion.

Citing Articles

Various microbial taxa couple arsenic transformation to nitrogen and carbon cycling in paddy soils.

Zhao X, Gao Z, Peng J, Konstantinidis K, Zhang S Microbiome. 2024; 12(1):238.

PMID: 39543780 PMC: 11566909. DOI: 10.1186/s40168-024-01952-4.


Sulfuricystis multivorans gen. nov., sp. nov. and Sulfuricystis thermophila sp. nov., facultatively autotropic sulfur-oxidizing bacteria isolated from a hot spring, and emended description of the genus Rugosibacter.

Kojima H, Watanabe M, Miyata N, Fukui M Arch Microbiol. 2022; 204(9):595.

PMID: 36053377 DOI: 10.1007/s00203-022-03186-0.


Microbial Oxidation of Arsenite: Regulation, Chemotaxis, Phosphate Metabolism and Energy Generation.

Shi K, Wang Q, Wang G Front Microbiol. 2020; 11:569282.

PMID: 33072028 PMC: 7533571. DOI: 10.3389/fmicb.2020.569282.

References
1.
Oremland R, Hoeft S, Santini J, Bano N, Hollibaugh R, Hollibaugh J . Anaerobic oxidation of arsenite in Mono Lake water and by a facultative, arsenite-oxidizing chemoautotroph, strain MLHE-1. Appl Environ Microbiol. 2002; 68(10):4795-802. PMC: 126446. DOI: 10.1128/AEM.68.10.4795-4802.2002. View

2.
Donahoe-Christiansen J, DImperio S, Jackson C, Inskeep W, McDermott T . Arsenite-oxidizing Hydrogenobaculum strain isolated from an acid-sulfate-chloride geothermal spring in Yellowstone National Park. Appl Environ Microbiol. 2004; 70(3):1865-8. PMC: 368298. DOI: 10.1128/AEM.70.3.1865-1868.2004. View

3.
Kwok S, Hodges R . Stabilizing and destabilizing clusters in the hydrophobic core of long two-stranded alpha-helical coiled-coils. J Biol Chem. 2004; 279(20):21576-88. DOI: 10.1074/jbc.M401074200. View

4.
Edgar R . MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 2004; 32(5):1792-7. PMC: 390337. DOI: 10.1093/nar/gkh340. View

5.
Bendtsen J, Nielsen H, Widdick D, Palmer T, Brunak S . Prediction of twin-arginine signal peptides. BMC Bioinformatics. 2005; 6:167. PMC: 1182353. DOI: 10.1186/1471-2105-6-167. View