Cubonová L'ubomíra, Surín Stanislav, Majerník Alan, Smigán Peter
Institute of Animal Biochemistry and Genetics, Slovak Academy of Sciences, 900 28 Ivanka pri Dunaji, Slovak Republic.
FEMS Microbiol Lett. 2004 Apr 1;233(1):23-8. doi: 10.1016/j.femsle.2004.01.033.
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.
分离出了嗜热栖热甲烷杆菌对质子载体解偶联剂TCS具有抗性的自发突变体。该突变菌株在非生长条件下表现出甲烷生成增加和ATP酶活性水平升高。在突变菌株中，由产甲烷电子传递以及在存在H⁺或Na⁺离子时由钾扩散电位驱动的ATP合成明显减少。在天然聚丙烯酰胺凝胶电泳后，在突变菌株中检测到一种分子量约为670 kDa的丰富的膜相关蛋白复合物。结果表明，该突变体对TCS的抗性是由于影响编码解偶联剂结合蛋白的特定基因座的突变和/或调节未鉴定ATP酶活性的突变所致。
