The sodium cycle. III. Vibrio alginolyticus resembles Vibrio cholerae and some other vibriones by flagellar motor and ribosomal 5S-RNA structures

Bakeeva, L. E.; Chumakov, Konstantin; Drachev, Alexander L.; Metlina, A. L.; Skulachev, Vladimir P.

doi:10.1016/0005-2728(86)90115-5

Cited by 41 publications

(11 citation statements)

References 35 publications

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“…Based on the analysis of 16S rRNA sequences (250,650,657), 5S rRNA sequences (33), and protein signature sequences (222) and phylogenetic analyses of several conserved proteins (475), D. radiodurans was found to be phylogenetically related to Thermus thermophilus. D. radiodurans and T. thermophilus have similar GC contents; are both naturally transformable, red pigmented, nonsporulating, and aerobic; and share an A3␤ murein-type peptidoglycan (L-ornithine as the diamino acid and glycylglycine as the interpeptide bridge) (249).…”

Section: Phylogeny Of D Radioduransmentioning

confidence: 99%

Oxidative Stress Resistance inDeinococcus radiodurans

Slade

Radman

2011

Microbiol Mol Biol Rev

648

639

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SUMMARY Deinococcus radiodurans is a robust bacterium best known for its capacity to repair massive DNA damage efficiently and accurately. It is extremely resistant to many DNA-damaging agents, including ionizing radiation and UV radiation (100 to 295 nm), desiccation, and mitomycin C, which induce oxidative damage not only to DNA but also to all cellular macromolecules via the production of reactive oxygen species. The extreme resilience of D. radiodurans to oxidative stress is imparted synergistically by an efficient protection of proteins against oxidative stress and an efficient DNA repair mechanism, enhanced by functional redundancies in both systems. D. radiodurans assets for the prevention of and recovery from oxidative stress are extensively reviewed here. Radiation- and desiccation-resistant bacteria such as D. radiodurans have substantially lower protein oxidation levels than do sensitive bacteria but have similar yields of DNA double-strand breaks. These findings challenge the concept of DNA as the primary target of radiation toxicity while advancing protein damage, and the protection of proteins against oxidative damage, as a new paradigm of radiation toxicity and survival. The protection of DNA repair and other proteins against oxidative damage is imparted by enzymatic and nonenzymatic antioxidant defense systems dominated by divalent manganese complexes. Given that oxidative stress caused by the accumulation of reactive oxygen species is associated with aging and cancer, a comprehensive outlook on D. radiodurans strategies of combating oxidative stress may open new avenues for antiaging and anticancer treatments. The study of the antioxidation protection in D. radiodurans is therefore of considerable potential interest for medicine and public health.

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Section: Phylogeny Of D Radioduransmentioning

confidence: 99%

Oxidative Stress Resistance inDeinococcus radiodurans

Slade

Radman

2011

Microbiol Mol Biol Rev

648

639

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“…Thus, at least in V. cholerae, a functional linkage between the virulence factor expression machinery and the Na ϩ cycle has been shown experimentally. The reason for this connection is not clear, although it has been speculated that one of the functions of cholera toxin might be the generation of an Na ϩ -rich environment in the intestinal lumen to boost the efficiency of the Na ϩ cycle in V. cholerae cells immersed in alkaline medium (9).…”

Section: Vibrio Choleraementioning

confidence: 99%

Sodium Ion Cycle in Bacterial Pathogens: Evidence from Cross-Genome Comparisons

Häse

Fedorova

Galperin

et al. 2001

Microbiol Mol Biol Rev

216

169

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Analysis of the bacterial genome sequences shows that many human and animal pathogens encode primary membrane Na+ pumps, Na+-transporting dicarboxylate decarboxylases or Na+-translocating NADH:ubiquinone oxidoreductase, and a number of Na+-dependent permeases. This indicates that these bacteria can utilize Na+ as a coupling ion instead of or in addition to the H+ cycle. This capability to use a Na+ cycle might be an important virulence factor for such pathogens as Vibrio cholerae, Neisseria meningitidis, Salmonella enterica serovar Typhi, and Yersinia pestis. In Treponema pallidum, Chlamydia trachomatis, and Chlamydia pneumoniae, the Na+ gradient may well be the only energy source for secondary transport. A survey of preliminary genome sequences of Porphyromonas gingivalis, Actinobacillus actinomycetemcomitans, and Treponema denticola indicates that these oral pathogens also rely on the Na+ cycle for at least part of their energy metabolism. The possible roles of the Na+ cycling in the energy metabolism and pathogenicity of these organisms are reviewed. The recent discovery of an effective natural antibiotic, korormicin, targeted against the Na+-translocating NADH:ubiquinone oxidoreductase, suggests a potential use of Na+ pumps as drug targets and/or vaccine candidates. The antimicrobial potential of other inhibitors of the Na+ cycle, such as monensin, Li+ and Ag+ ions, and amiloride derivatives, is discussed

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“…The MotA/MotB complex of Escherichia coli is an H + -driven flagellar motor. In contrast, alkaliphilic Bacillus species or marine bacteria such as Vibrio species have MotP/MotS or PomA/PomB complexes that are Na + -driven flagellar motors (Manson et al, 1977;Bakeeva et al, 1986;Macnab, 1999;Berg, 2003;Blair, 2003;Li et al, 2011). Dual ion-coupling capacity is found in neutralophilic Bacillus subtilis with both MotA/MotB and MotP/MotS (Ito et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Suppressor mutants from MotB-D24E and MotS-D30E in the flagellar stator complex of Bacillus subtilis

Takahashi

Koyama

Ito

2014

J. Gen. Appl. Microbiol.

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The bacterial flagellar motor is mainly energized by either a proton (H + ) or sodium ion (Na + ) motive force and the motor torque is generated by interaction at the rotor-stator interface. MotA/MotB-type stators use H + as the coupling ion, whereas MotP/ MotS-and PomA/PomB-type stators use Na + . Bacillus subtilis employs both H + -coupled MotA/MotB and Na + -coupled MotP/MotS stators, which contribute to the torque required for flagellar rotation. In Escherichia coli, there is a universally conserved Asp-32 residue of MotB that is critical for motility and is a predicted H + -binding site. In B. subtilis, the conserved aspartic acid residue corresponds to Asp-24 of MotB (MotB-D24) and Asp-30 of MotS (MotS-D30). Here we report the isolation of two mutants, MotB-D24E and MotS-D30E, which showed a nonmotile and poorly motile phenotype, respectively. Up-motile mutants were spontaneously isolated from each mutant. We identified a suppressor mutation at MotB-T181A and MotP-L172P, respectively. Mutants MotB-T181A and MotP-L172P showed about 50% motility and a poorly motile phenotype compared to each wild type strain. These suppressor sites were suggested to indirectly affect the structure of the ion influx pathway.

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The sodium cycle. III. Vibrio alginolyticus resembles Vibrio cholerae and some other vibriones by flagellar motor and ribosomal 5S-RNA structures

Cited by 41 publications

References 35 publications

Oxidative Stress Resistance inDeinococcus radiodurans

Oxidative Stress Resistance inDeinococcus radiodurans

Sodium Ion Cycle in Bacterial Pathogens: Evidence from Cross-Genome Comparisons

Suppressor mutants from MotB-D24E and MotS-D30E in the flagellar stator complex of Bacillus subtilis

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