Isolation and characterization of a N,N'-dicyclohexylcarbodiimide-resistant mutant of Methanothermobacter thermautotrophicus with alterations to the ATP synthesis machinery
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Adenosine Triphosphate metabolism MeSH
- Archaeal Proteins biosynthesis MeSH
- Dicyclohexylcarbodiimide toxicity MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Gene Expression MeSH
- Enzyme Inhibitors toxicity MeSH
- Drug Resistance * MeSH
- Methane metabolism MeSH
- Methanobacteriaceae chemistry drug effects isolation & purification metabolism MeSH
- Mutation * MeSH
- Oxidation-Reduction MeSH
- Proton-Translocating ATPases biosynthesis MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MeSH
- Up-Regulation MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Adenosine Triphosphate MeSH
- Archaeal Proteins MeSH
- Dicyclohexylcarbodiimide MeSH
- Enzyme Inhibitors MeSH
- Methane MeSH
- Proton-Translocating ATPases MeSH
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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