A shaE deletion mutant showed lower Na+ sensitivity compound to other deletion mutants in the Bacillus subtilis sodium/hydrogen antiporter (Sha) system

Yoshinaka, Toko; Takasu, Hirotoshi; Tomizawa, Rui; Kosono, Saori; Kudo, Toshiaki

doi:10.1016/s1389-1723(03)80035-x

Cited by 17 publications

(5 citation statements)

References 13 publications

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“…and Synechococcus elongatus (Blanco-Rivero et al, 2005;Cui et al, 2020), among others. Besides, Mrp antiporters (also known as Sha/Mnh/Pha) seem to contribute to the sporulation process (Kosono et al, 2000;Sun and Shi, 2001;Yoshinaka et al, 2003), which has been observed in the morphology of seven-day-old cells of strains 3ASR75-54 T , 3ASR75-11 T , 3ASR75-286, and the species of the genus Aquibacillus and Radiobacillus (Lee et al, 2006;Zhang et al, 2012Zhang et al, , 2015Amoozegar et al, 2014;Lee and Whang, 2019;Li et al, 2020;Wang et al, 2021;Cho and Whang, 2022). Additionally, the ChaA antiporter (K07300), which has a relevant role in the extrusion of Na + in Escherichia coli (Ohyama et al, 1994), has been found in the annotated genome of Although ion exchange is useful as a first barrier of defense against osmotic pressure, it is more convenient to store compatible solutes into the cytoplasm for prolonged periods of stress Bremer, 2016, 2017).…”

Section: Mechanisms Detected For Survival In Hypersaline Environmentsmentioning

confidence: 99%

A step into the rare biosphere: genomic features of the new genus Terrihalobacillus and the new species Aquibacillus salsiterrae from hypersaline soils

et al. 2023

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Hypersaline soils are a source of prokaryotic diversity that has been overlooked until very recently. The phylum Bacillota, which includes the genus Aquibacillus, is one of the 26 phyla that inhabit the heavy metal contaminated soils of the Odiel Saltmarshers Natural Area (Southwest Spain), according to previous research. In this study, we isolated a total of 32 strains closely related to the genus Aquibacillus by the traditional dilution-plating technique. Phylogenetic studies clustered them into two groups, and comparative genomic analyses revealed that one of them represents a new species within the genus Aquibacillus, whereas the other cluster constitutes a novel genus of the family Bacillaceae. We propose the designations Aquibacillus salsiterrae sp. nov. and Terrihalobacillus insolitus gen. nov., sp. nov., respectively, for these two new taxa. Genome mining analysis revealed dissimilitude in the metabolic traits of the isolates and their closest related genera, remarkably the distinctive presence of the well-conserved pathway for the biosynthesis of molybdenum cofactor in the species of the genera Aquibacillus and Terrihalobacillus, along with genes that encode molybdoenzymes and molybdate transporters, scarcely found in metagenomic dataset from this area. In-silico studies of the osmoregulatory strategy revealed a salt-out mechanism in the new species, which harbor the genes for biosynthesis and transport of the compatible solutes ectoine and glycine betaine. Comparative genomics showed genes related to heavy metal resistance, which seem required due to the contamination in the sampling area. The low values in the genome recruitment analysis indicate that the new species of the two genera, Terrihalobacillus and Aquibacillus, belong to the rare biosphere of representative hypersaline environments.

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Section: Mechanisms Detected For Survival In Hypersaline Environmentsmentioning

confidence: 99%

A step into the rare biosphere: genomic features of the new genus Terrihalobacillus and the new species Aquibacillus salsiterrae from hypersaline soils

et al. 2023

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“…By contrast, the MrpE subunit appears to be incorporated in the final step of complex formation and possibly plays an important role in ensuring that the Mrp complex can exert its full activity. However, in B. subtilis , it was reported that MrpE is dispensable for ion transport activity ( Yoshinaka et al, 2003 ; Morino et al, 2008 ).…”

Section: Features Of the Mrp Antiporter From Alkaliphilic Bmentioning

confidence: 99%

“…Various mrp -deficient strains have been produced in B. subtilis , and it has been reported from their analysis that the mrpF gene contributes to bile acid tolerance ( Ito et al, 1999 ). Furthermore, it has been reported that sodium efflux capacity is retained in a mrpE gene-deficient strain ( Yoshinaka et al, 2003 ; Morino et al, 2008 ). S. aureus Mrp is expected to be a target protein of a novel antibiotic because since growth inhibition of S. aureus is suppressed by inhibiting translation of the mrpD gene using antisense RNA ( Ji et al, 2001 ).…”

Section: Mrp Antiporters From Gram-positive Bacteria Other Than Alkalmentioning

confidence: 99%

Mrp Antiporters Have Important Roles in Diverse Bacteria and Archaea

2017

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Mrp (Multiple resistance and pH) antiporter was identified as a gene complementing an alkaline-sensitive mutant strain of alkaliphilic Bacillus halodurans C-125 in 1990. At that time, there was no example of a multi-subunit type Na+/H+ antiporter comprising six or seven hydrophobic proteins, and it was newly designated as the monovalent cation: proton antiporter-3 (CPA3) family in the classification of transporters. The Mrp antiporter is broadly distributed among bacteria and archaea, not only in alkaliphiles. Generally, all Mrp subunits, mrpA–G, are required for enzymatic activity. Two exceptions are Mrp from the archaea Methanosarcina acetivorans and the eubacteria Natranaerobius thermophilus, which are reported to sustain Na+/H+ antiport activity with the MrpA subunit alone. Two large subunits of the Mrp antiporter, MrpA and MrpD, are homologous to membrane-embedded subunits of the respiratory chain complex I, NuoL, NuoM, and NuoN, and the small subunit MrpC has homology with NuoK. The functions of the Mrp antiporter include sodium tolerance and pH homeostasis in an alkaline environment, nitrogen fixation in Schizolobium meliloti, bile salt tolerance in Bacillus subtilis and Vibrio cholerae, arsenic oxidation in Agrobacterium tumefaciens, pathogenesis in Pseudomonas aeruginosa and Staphylococcus aureus, and the conversion of energy involved in metabolism and hydrogen production in archaea. In addition, some Mrp antiporters transport K+ and Ca2+ instead of Na+, depending on the environmental conditions. Recently, the molecular structure of the respiratory chain complex I has been elucidated by others, and details of the mechanism by which it transports protons are being clarified. Based on this, several hypotheses concerning the substrate transport mechanism in the Mrp antiporter have been proposed. The MrpA and MrpD subunits, which are homologous to the proton transport subunit of complex I, are involved in the transport of protons and their coupling cations. Herein, we outline other recent findings on the Mrp antiporter.

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“…In contrast, the CPA3 family of antiporters, which are commonly referred to by the name of the initial example, Mrp (10), are the products of operons that carry either seven genes, the mrpA to -G genes, or six genes, the mrpA= to -G genes, in which MrpA= is a fused version of MrpA and MrpB (11). All of the genes are required for full activity, and all but MrpE are required for any significant activity (12)(13)(14)(15). Studies of seven-subunit Bacillus Mrp antiporters show that they form hetero-oligomeric complexes containing all seven subunits, and the active form of Mrp appears to be a dimer of the hetero-oligomeric Mrp complex (15,16).…”

mentioning

confidence: 99%

Purification and Functional Reconstitution of a Seven-Subunit Mrp-Type Na+/H+ Antiporter

Morino

Suzuki

Ito

et al. 2013

Journal of Bacteriology

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Mrp antiporters and their homologues in the cation/proton antiporter 3 family of the Membrane Transporter Database are widely distributed in bacteria. They have major roles in supporting cation and cytoplasmic pH homeostasis in many environmental, extremophilic, and pathogenic bacteria. These antiporters require six or seven hydrophobic proteins that form heterooligomeric complexes, while most other cation/proton antiporters require only one membrane protein for their activity. The resemblance of three Mrp subunits to membrane-embedded subunits of the NADH:quinone oxidoreductase of respiratory chains and to subunits of several hydrogenases has raised interest in the evolutionary path and commonalities of their protontranslocating domains. In order to move toward a greater mechanistic understanding of these unusual antiporters and to rigorously demonstrate that they function as secondary antiporters, powered by an imposed proton motive force, we established a method for purification and functional reconstitution of the seven-subunit Mrp antiporter from alkaliphilic Bacillus pseudofirmus OF4. Na ؉ /H ؉ antiporter activity was demonstrated by a fluorescence-based assay with proteoliposomes in which the Mrp complex was coreconstituted with a bacterial F o F 1 -ATPase. Proton pumping by the ATPase upon addition of ATP generated a proton motive force across the membranes that powered antiporter activity upon subsequent addition of Na ؉ .

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A shaE deletion mutant showed lower Na+ sensitivity compound to other deletion mutants in the Bacillus subtilis sodium/hydrogen antiporter (Sha) system

Cited by 17 publications

References 13 publications

A step into the rare biosphere: genomic features of the new genus Terrihalobacillus and the new species Aquibacillus salsiterrae from hypersaline soils

A step into the rare biosphere: genomic features of the new genus Terrihalobacillus and the new species Aquibacillus salsiterrae from hypersaline soils

Mrp Antiporters Have Important Roles in Diverse Bacteria and Archaea

Purification and Functional Reconstitution of a Seven-Subunit Mrp-Type Na+/H+ Antiporter

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