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A magnesium transporter is involved in the cesium ion resistance of the high-concentration cesium ion-resistant bacterium Microbacterium sp. TS-1.

ABSTRACT: Cesium ion (Cs⁺) resistance has been reported in bacteria but is poorly understood as reports on Cs⁺-resistant bacteria have been limited. We previously reported a novel Cs⁺/H⁺ antiporter CshA implicated in Cs⁺-resistance in Microbacterium sp. TS-1. The present study used the same screening method to isolate novel Cs⁺-sensitive mutants and their revertants from TS-1. A comparative mutation site analysis using whole-genome sequencing revealed that MTS1_03028 encodes the Mg²⁺ transporter MgtE and is a candidate Cs⁺ resistance-related gene. We performed a bioinformatic analysis of MTS1_03028 and complementation experiments on Cs⁺ resistance in the TS-1 MTS1_03028 mutants Mut5 and Mut7 as well as Escherichia coli expressing MTS1_03028 in the presence of Mg²⁺. We established the role of MgtE in Cs⁺ resistance through a functional analysis of TS-1. Enhancing Mg²⁺ transport by expression of MTS_03028 conferred increased Cs⁺ resistance. When this strain was exposed to Cs⁺ concentrations exceeding 200 mM, CshA consistently lowered the intracellular Cs⁺ concentration. To our knowledge, the present study is the first to clarify the mechanism of Cs⁺ resistance in certain bacteria. The study findings offer important insights into the mechanism of bacterial resistance to excess Cs⁺ in the environment, suggesting the potential for bioremediation in high Cs-contaminated areas.

SUBMITTER: Ishida Y

PROVIDER: S-EPMC9995610 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature

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A magnesium transporter is involved in the cesium ion resistance of the high-concentration cesium ion-resistant bacterium Microbacterium sp. TS-1.

Ishida Yoshiki Y Koretsune Takahiro T Ishiuchi Eri E Teshima Miyu M Ito Masahiro M

Frontiers in microbiology 20230223

Cesium ion (Cs+) resistance has been reported in bacteria but is poorly understood as reports on Cs+-resistant bacteria have been limited. We previously reported a novel Cs+/H+ antiporter CshA implicated in Cs+-resistance in Microbacterium sp. TS-1. The present study used the same screening method to isolate novel Cs+-sensitive mutants and their revertants from TS-1. A comparative mutation site analysis using whole-genome s ...[more]

PMID: 36910217

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Project description:Under general aqueous conditions, xanthan appears in an ordered conformation, which makes its backbone largely resistant to degradation by known cellulases. Therefore, the xanthan degradation mechanism is still unclear because of the lack of an efficient hydrolase. Here, we report the catalytic properties of MiXen, a xanthan-degrading enzyme identified from the genus Microbacterium MiXen is a 952-amino-acid protein that is unique to strain XT11. Both the sequence and structural features suggested that MiXen belongs to a new branch of the GH9 family and has a multimodular structure in which a catalytic (α/α)6 barrel is flanked by an N-terminal Ig-like domain and by a C-terminal domain that has very few homologues in sequence databases and functions as a carbohydrate-binding module (CBM). Based on circular dichroism, shear-dependent viscosity, and reducing sugar and gel permeation chromatography analysis, we demonstrated that recombinant MiXen efficiently and randomly cleaved glucosidic bonds within the highly ordered xanthan substrate. A MiXen mutant free of the C-terminal CBM domain partially lost its xanthan-hydrolyzing ability because of decreased affinity toward xanthan, indicating the CBM domain assisted MiXen in hydrolyzing highly ordered xanthan via recognizing and binding to the substrate. Furthermore, side chain substituents and the terminal mannosyl residue significantly influenced the activity of MiXen via the formation of barriers to enzymolysis. Overall, the results of this study provide insight into the hydrolysis mechanism and enzymatic properties of a novel endotype xanthanase that will benefit future applications.IMPORTANCE This work characterized a novel endotype xanthanase, MiXen, and elucidated that the C-terminal carbohydrate-binding module of MiXen could drastically enhance the hydrolysis activity of the enzyme toward highly ordered xanthan. Both the sequence and structural analysis demonstrated that the catalytic domain and carbohydrate-binding module of MiXen belong to the novel branch of the GH9 family and CBMs, respectively. This xanthan cleaver can help further reveal the enzymolysis mechanism of xanthan and provide an efficient tool for the production of molecular modified xanthan with new physicochemical and physiological functions.

Dataset Information

A magnesium transporter is involved in the cesium ion resistance of the high-concentration cesium ion-resistant bacterium Microbacterium sp. TS-1.

Publications

A magnesium transporter is involved in the cesium ion resistance of the high-concentration cesium ion-resistant bacterium <i>Microbacterium</i> sp. TS-1.

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