Isolation and characterization of a N,N'-dicyclohexylcarbodiimide-resistant mutant of Methanothermobacter thermautotrophicus with alterations to the ATP synthesis machinery
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- adenosintrifosfát metabolismus MeSH
- archeální proteiny biosyntéza MeSH
- dicyklohexylkarbodiimid toxicita MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- exprese genu MeSH
- inhibitory enzymů toxicita MeSH
- léková rezistence * MeSH
- methan metabolismus MeSH
- Methanobacteriaceae chemie účinky léků izolace a purifikace metabolismus MeSH
- mutace * MeSH
- oxidace-redukce MeSH
- protonové ATPasy biosyntéza MeSH
- spektrometrie hmotnostní - ionizace laserem za účasti matrice MeSH
- upregulace MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- adenosintrifosfát MeSH
- archeální proteiny MeSH
- dicyklohexylkarbodiimid MeSH
- inhibitory enzymů MeSH
- methan MeSH
- protonové ATPasy 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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