| Autor: |
Nováková, Zuzana, Bobálová, Janette, Vidová, Monika, Hapala, Ivan, Šmigáň, Peter |
| Předmět: |
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| Zdroj: |
FEMS Microbiology Letters; Sep2009, Vol. 298 Issue 2, p255-259, 5p, 3 Graphs |
| Abstrakt: |
A spontaneous mutant of Methanothermobacter thermautotrophicus resistant to tributyltin chloride (TBT) was isolated. TBT, the inhibitor of the A0 domain of A1A0-ATP synthase, inhibits methanogenesis in the wild-type cells; however, the TBT-resistant mutant exhibited methanogenesis even in the presence of 800 μM TBT. ATP synthesis driven by methanogenic electron transport was markedly diminished in the mutant strain. While TBT profoundly inhibited ATP synthesis driven by methanogenic electron transport in the wild type, only a slight inhibition was observed in the mutant strain. These results suggested a modification in the ATP-synthesizing system of the mutant strain. The sequence of the complete A1A0-ATP synthase operon ( Mth952– Mth961) in the wild-type and mutant strains was determined and compared. Three mutations leading to amino acid substitutions in two A1A0-ATP synthase subunits were identified – Val338Ala in subunit A and Leu252Ile and Ser293Ala in subunit B. Moreover, this study revealed the differential expression of several proteins that may contribute to TBT resistance. The results imply that change of TBT sensitivities of TBT-resistant mutant is due to mutational substitutions in the A1A0-ATP synthase operon. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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