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 Journal of Biological Chemistry
Masato MorinoMasahiro Ito

Abstract

Mrp systems are widely distributed and structurally complex cation/proton antiporters. Antiport activity requires hetero-oligomeric complexes of all six or seven hydrophobic Mrp proteins (MrpA-MrpG). Here, a panel of site-directed mutants in conserved or proposed motif residues was made in the Mrp Na(+)(Li(+))/H(+) antiporter from an alkaliphilic Bacillus. The mutant operons were expressed in antiporter-deficient Escherichia coli KNabc and assessed for antiport properties, support of sodium resistance, membrane levels of each Mrp protein, and presence of monomeric and dimeric Mrp complexes. Antiport did not depend on a VFF motif or a conserved tyrosine pair, but a role for a conserved histidine in a potential quinone binding site of MrpA was supported. The importance of several acidic residues for antiport was confirmed, and the importance of additional residues was demonstrated (e.g. three lysine residues conserved across MrpA, MrpD, and membrane-bound respiratory Complex I subunits (NuoL/M/N)). The results extended indications that MrpE is required for normal membrane levels of other Mrp proteins and for complex formation. Moreover, mutations in several other Mrp proteins lead to greatly reduced membrane levels of MrpE. Thus,...Continue Reading

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Citations

Apr 6, 2011·Nature Reviews. Microbiology·Terry A KrulwichEtana Padan
Jul 10, 2013·Journal of Bacteriology·Ricardo Jasso-ChávezJames G Ferry
Oct 22, 2013·Journal of Bacteriology·Masato MorinoTerry Ann Krulwich
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Dec 7, 2020·Journal of Molecular Biology·Li ShaoJuquan Jiang
May 15, 2018·Cell·Hongjun YuHuilin Li
May 7, 2021·The Journal of Biological Chemistry·Hongjun YuHuilin Li

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