Na<sup>+</sup>‐driven ATP synthesis in <i>Methanobacterium thermoautotrophicum</i> can be modulated with sodium ion concentrations in the growth medium

Šmigáň, P.; Horovská, Ľubica; Greksák, M

doi:10.1016/0014-5793(88)80990-6

Cited by 23 publications

(3 citation statements)

References 26 publications

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“…It seems likely that mutant cells contain a newly induced ATPase of unknown function. The existence of an inducible ATPase in M. thermautotrophicus cells was previously suggested by our group [28]. Hence, the observed increase in ATP hydrolysis and the lowered ATP synthesis in the mutant strain might indicate that uncoupler resistance arose from a mutation affecting an activity of some yet unidentified drug efflux ATPase which could be driven by ATP hydrolysis – ATP binding cassette (ABC) multidrug transporter [30].…”

Section: Discussionmentioning

confidence: 86%

Isolation and characterization of an uncoupler-resistant mutant ofMethanothermobacter thermautotrophicus

Čuboňová

Šurín

Majerník

et al. 2004

FEMS Microbiology Letters

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A spontaneous mutant of Methanothermobacter thermautotrophicus resistant to the protonophorous uncoupler TCS was isolated. The mutant strain exhibited increased CH(4) formation and elevated level of ATPase activity under non-growing conditions. ATP synthesis driven by methanogenic electron transport as well as by potassium diffusion potential in the presence of either H(+) or Na(+) ions was markedly diminished in the mutant strain. An abundant membrane-associated protein complex with molecular mass approximately 670 kDa was detected in the mutant strain after native PAGE. The results indicate that TCS resistance in this mutant has arisen as a consequence of mutation(s) that affects a specific locus coding for an uncoupler binding protein(s) and/or modulate the activity of unidentified ATPase.

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Section: Discussionmentioning

confidence: 86%

Isolation and characterization of an uncoupler-resistant mutant ofMethanothermobacter thermautotrophicus

Čuboňová

Šurín

Majerník

et al. 2004

FEMS Microbiology Letters

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“…Several methanoarchaea, including methylotropic (M. barkeri), hydrogenotropic and halophilic methanogens (Methanohalophilus halophilus) were shown to be sensitive to DCCD, suggesting that M. thermautotrophicus may also encode one or more DCCD-sensitive ATPases (Doddema et al 1978;Blaut et al 1984;Šmigáň et al 1988, 1992. A DCCD-resistant mutant can be expected to alter the ATP synthase itself, thus offering a potential tool to study the ATP-synthesizing machinery in methanoarchaea.…”

Section: Abbreviationsmentioning

confidence: 97%

Isolation and characterization of a N,N′-dicyclohexylcarbodiimide-resistant mutant of Methanothermobacter thermautotrophicus with alterations to the ATP synthesis machinery

et al. 2009

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A spontaneous mutant of Methanothermobacter thermautotrophicus resistant toward the ATP-synthase inhibitor N,N'-dicyclohexylcarbodiimide (DCCD) was isolated. DCCD normally inhibits methanogenic electron-transport-driven ATP synthesis, however, the DCCD-resistant strain exhibited methanogenesis in the presence of 300 micromol/L DCCD. Total ATP synthesis was shown to be higher in the mutant strain, both in the presence and absence of DCCD. These results suggested a modification in the ATP-synthesizing system of the mutant strain. Using Blue Native PAGE combined with MALDI TOF/TOF mass spectrometry, increased concentrations of both the A(1) and A(o) subcomplexes of the A(1)A(o)-type synthase were identified in the mutant strain. However, no alterations were found in the structural genes (atp) for the A(1)A(o) ATP synthase. The results imply that DCCD resistance is a consequence of increased A(1)A(o) ATP synthase expression, and suggest that genes involved in regulating synthase expression are responsible for DCCD resistance.

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“…The observation that Na + ‐translocating ATPase (synthase) in Mb. thermoautotrophicum is inductive [16]could permit modulation of its activity at different physiological conditions. Moreover, this ATPase (synthase) seems to be F‐type ATPase [12, 13].…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterization of a neomycin‐resistant mutant of Methanobacterium thermoautotrophicum with a lesion in Na⁺‐translocating ATPase (synthase)

et al. 1997

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A mutant of Methanobacterium thermoautotrophicum with a lesion in membrane Na + -translocating ATPase (synthase) was isolated. The total ATPase activity in permeabilized cells of this mutant was elevated three-fold as compared with the wild-type strain. In contrast to wild-type cells, mutant ATPase was neither inhibited by DCCD nor stimulated by Na + ions. The methane formation orate of the mutant cells at pH 7.5 under non-growing conditions was nearly twice that of the wildtype strain and was stimulated by sodium ions. On the other hand, the ATP synthesis driven by methanogenesis under the same conditions was lower that of the wild-type under the same conditions, and contrary to the wild-type was not stimulated by Na + ions. ATP synthesis driven by a potassium diffusion potential in the presence of sodium ions was markedly diminished in the mutant cells. The membrane potential values of the wildtype and the mutant cells in the presence of 10 mM NaCl at pH 7.0 were comparable at energized conditions (3223 mV and 3230 mV respectively). The Mg 2+ -dependent ATPase activity of the 10 S Ug supernatant of broken cells from the mutant cells was 30% higher than in the wild-type. On the other hand, two bands with Mg 2+ -dependent ATPase activity were identified by native PAGE in this fraction in both wild-type as well as in mutant. These data suggest that the binding of Na + -translocating ATPase (synthase) to the membrane spanning part is changed in the mutant strain.z 1997 Federation of European Biochemical Societies.

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Na⁺‐driven ATP synthesis in Methanobacterium thermoautotrophicum can be modulated with sodium ion concentrations in the growth medium

Cited by 23 publications

References 26 publications

Isolation and characterization of an uncoupler-resistant mutant ofMethanothermobacter thermautotrophicus

Isolation and characterization of an uncoupler-resistant mutant ofMethanothermobacter thermautotrophicus

Isolation and characterization of a N,N′-dicyclohexylcarbodiimide-resistant mutant of Methanothermobacter thermautotrophicus with alterations to the ATP synthesis machinery

Isolation and characterization of a neomycin‐resistant mutant of Methanobacterium thermoautotrophicum with a lesion in Na⁺‐translocating ATPase (synthase)

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Na+‐driven ATP synthesis in Methanobacterium thermoautotrophicum can be modulated with sodium ion concentrations in the growth medium

Cited by 23 publications

References 26 publications

Isolation and characterization of an uncoupler-resistant mutant ofMethanothermobacter thermautotrophicus

Isolation and characterization of an uncoupler-resistant mutant ofMethanothermobacter thermautotrophicus

Isolation and characterization of a N,N′-dicyclohexylcarbodiimide-resistant mutant of Methanothermobacter thermautotrophicus with alterations to the ATP synthesis machinery

Isolation and characterization of a neomycin‐resistant mutant of Methanobacterium thermoautotrophicum with a lesion in Na+‐translocating ATPase (synthase)

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Na⁺‐driven ATP synthesis in Methanobacterium thermoautotrophicum can be modulated with sodium ion concentrations in the growth medium

Isolation and characterization of a neomycin‐resistant mutant of Methanobacterium thermoautotrophicum with a lesion in Na⁺‐translocating ATPase (synthase)