Effect of 2,4-dinitrophenol and ionophores on growth and methanogenesis inMethanobacterium thermoautotrophicum

Šmigáň, P.; Friederová, A.; Rusňák, P.; Greksák, M

doi:10.1007/bf02887762

Cited by 19 publications

(10 citation statements)

References 17 publications

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“…Cultures of ATCC29096 were obtained again in 2005 from the ATCC, and from the German Microbiology Culture Collection (designated DSMZ strain 1053). A culture of an independent M. thermoautotrophicum isolate, separately deposited and now designated M. thermautotrophicus ATCC29183 was provided by Šmigán et al (1984). This lineage was originally obtained from the ATCC in 1980 (Sauer et al 1980).…”

Section: Methodsmentioning

confidence: 99%

Archaeal chromatin proteins histone HMtB and Alba have lost DNA-binding ability in laboratory strains of Methanothermobacter thermautotrophicus

et al. 2008

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Alignments of the sequences of the all members of the archaeal histone and Alba1 families of chromatin proteins identified isoleucine residues, I19 in HMtB and I39 in MtAlba, in Methanothermobacter thermautotrophicus, at locations predicted to be directly involved in DNA binding. In all other HMfB family members, residue 19 is an arginine (R19), and either arginine or lysine is present in almost all other Alba1 family members at the structural site equivalent to I39 in MtAlba. Electrophoretic mobility shift assays revealed that recombinant HMtB and MtAlba do not bind DNA, but variants constructed with R19 and R39, respectively, bound DNA; and whereas MtAlba(I19) did not bind RNA, MtAlba(R19) bound both single stranded RNA and tRNA. Amplification and sequencing of MT0254 (encodes HMtB) and MT1483 (encodes MtAlba) from several Methanothermobacter thermautotrophicus lineages has revealed that HMtB and MtAlba had arginine residues at positions 19 and 39, respectively, in the original isolate and that spontaneous mutations must have occurred, and been fixed, in some laboratory lineages that now have HMtB(I19) and MtAlba(I39). The retention of these variants suggests some continuing functions and fusion of the HMtB(I19) sequence to HMtA2 resulted in a protein that folds to form a histone fold heterodimer that binds and compacts DNA. The loss of DNA binding by HMtB(I19) does not therefore prevent HMtB from participating in DNA interactions as one partner of an archaeal histone heterodimer.

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Section: Methodsmentioning

confidence: 99%

Archaeal chromatin proteins histone HMtB and Alba have lost DNA-binding ability in laboratory strains of Methanothermobacter thermautotrophicus

et al. 2008

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“…Methanothermobacter thermautotrophicus and its TCS‐resistant mutant were cultivated as described earlier [19]. Solid media were prepared by the addition of 1% (w/v) Gelrite to the medium.…”

Section: Methodsmentioning

confidence: 99%

“…All manipulations were performed under strict anaerobic conditions. For isolation of the uncoupler‐resistant mutant of M. thermautotrophicus , the growth medium [19] contained K 2 CO 3 instead of Na 2 CO 3 and was supplemented with 5 mM NaCl (Na + /K + ratio 1/6). To select uncoupler TCS‐resistant mutants, cultures were grown for 24 h in liquid medium in the presence of 5 μM TCS (Kodak).…”

Section: Methodsmentioning

confidence: 99%

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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“…Mb. thermoautotrophicum strain ΔH was used as a wild‐type strain and cultivated as described previously [19]. Growth medium was buffered to pH 7.5 with 50 mM morpholinopropane sulfonic acid (MOPS)‐KOH.…”

Section: Methodsmentioning

confidence: 99%

“…Methane formation from CO 2 and H 2 by the cell suspension of the wild‐type and neomycin‐resistant mutant was measured by gas chromatography as described earlier [19]. Samples of the gaseous phase were taken from cultivation flasks (5 ml bottles sealed with butyl‐rubber stoppers) with gas‐tight syringes.…”

Section: Methodsmentioning

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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Effect of 2,4-dinitrophenol and ionophores on growth and methanogenesis inMethanobacterium thermoautotrophicum

Cited by 19 publications

References 17 publications

Archaeal chromatin proteins histone HMtB and Alba have lost DNA-binding ability in laboratory strains of Methanothermobacter thermautotrophicus

Archaeal chromatin proteins histone HMtB and Alba have lost DNA-binding ability in laboratory strains of Methanothermobacter thermautotrophicus

Isolation and characterization of an uncoupler-resistant mutant ofMethanothermobacter thermautotrophicus

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

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Effect of 2,4-dinitrophenol and ionophores on growth and methanogenesis inMethanobacterium thermoautotrophicum

Cited by 19 publications

References 17 publications

Archaeal chromatin proteins histone HMtB and Alba have lost DNA-binding ability in laboratory strains of Methanothermobacter thermautotrophicus

Archaeal chromatin proteins histone HMtB and Alba have lost DNA-binding ability in laboratory strains of Methanothermobacter thermautotrophicus

Isolation and characterization of an uncoupler-resistant mutant ofMethanothermobacter thermautotrophicus

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

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