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Characterization of Bacillus subtilis YfkE (ChaA): a calcium-specific Ca2+/H+ antiporter of the CaCA familyMutations alter the sodium versus proton use of a Bacillus clausii flagellar motor and confer dual ion use on Bacillus subtilis motors.A Bacillus flagellar motor that can use both Na+ and K+ as a coupling ion is converted by a single mutation to use only Na+The Mrp Na+/H+ antiporter increases the activity of the malate:quinone oxidoreductase of an Escherichia coli respiratory mutant.Bacillus subtilis YqkI is a novel malic/Na+-lactate antiporter that enhances growth on malate at low protonmotive force.Effects of nonpolar mutations in each of the seven Bacillus subtilis mrp genes suggest complex interactions among the gene products in support of Na(+) and alkali but not cholate resistance.The activity profile of the NhaD-type Na+(Li+)/H+ antiporter from the soda Lake Haloalkaliphile Alkalimonas amylolytica is adaptive for the extreme environment.Single site mutations in the hetero-oligomeric Mrp antiporter from alkaliphilic Bacillus pseudofirmus OF4 that affect Na+/H+ antiport activity, sodium exclusion, individual Mrp protein levels, or Mrp complex formation.The Na(+)-dependence of alkaliphily in Bacillus.Ionic selectivity and thermal adaptations within the voltage-gated sodium channel family of alkaliphilic Bacillus.Motility and chemotaxis in alkaliphilic Bacillus species.Three two-component transporters with channel-like properties have monovalent cation/proton antiport activityGenome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that support the ability to grow in an external pH range from 7.5 to 11.4.Catalytic properties of Staphylococcus aureus and Bacillus members of the secondary cation/proton antiporter-3 (Mrp) family are revealed by an optimized assay in an Escherichia coli host.Single gene deletions of mrpA to mrpG and mrpE point mutations affect activity of the Mrp Na+/H+ antiporter of alkaliphilic Bacillus and formation of hetero-oligomeric Mrp complexesThe voltage-gated Na+ channel NaVBP co-localizes with methyl-accepting chemotaxis protein at cell poles of alkaliphilic Bacillus pseudofirmus OF4.Purification and functional reconstitution of a seven-subunit mrp-type na+/h+ antiporter.Energetic problems of extremely alkaliphilic aerobes.Cation/proton antiporter complements of bacteria: why so large and diverse?A novel type bacterial flagellar motor that can use divalent cations as a coupling ion.Functional expression of the multi-subunit type calcium/proton antiporter from Thermomicrobium roseum.The relationship between a coiled morphology and Mbl in alkaliphilic Bacillus halodurans C-125 at neutral pH values.Mrp-dependent Na(+)/H(+) antiporters of Bacillus exhibit characteristics that are unanticipated for completely secondary active transporters.Suppressor mutants from MotB-D24E and MotS-D30E in the flagellar stator complex of Bacillus subtilis.Modulation of the K+ efflux activity of Bacillus subtilis YhaU by YhaT and the C-terminal region of YhaS.Mutational analysis of charged residues in the cytoplasmic loops of MotA and MotP in the Bacillus subtilis flagellar motor.NhaK, a novel monovalent cation/H+ antiporter of Bacillus subtilis.Draft Genome Sequence of Calcium-Dependent Novosphingobium sp. Strain TCA1, Isolated from a Hot Spring Containing a High Concentration of Calcium IonsA Factor Produced by Kaistia sp. 32K Accelerated the Motility of Methylobacterium sp. ME121MotP Subunit is Critical for Ion Selectivity and Evolution of a K+-Coupled Flagellar Motor
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description
researcher ORCID: 0000-0002-4976-762X
@en
name
Masahiro Ito
@ast
Masahiro Ito
@en
Masahiro Ito
@es
Masahiro Ito
@nl
type
label
Masahiro Ito
@ast
Masahiro Ito
@en
Masahiro Ito
@es
Masahiro Ito
@nl
prefLabel
Masahiro Ito
@ast
Masahiro Ito
@en
Masahiro Ito
@es
Masahiro Ito
@nl
P106
P21
P31
P496
0000-0002-4976-762X