PMID: 15227786Jul 2, 2004Paper

Biochemical characteristics of a mutant of the methanoarchaeon Methanothermobacter thermautotrophicus resistant to the protonophoric uncoupler TCS

Folia Microbiologica
L CijbonováP Smigán

Abstract

In an attempt to more closely define a protein basis of differences in ATPase and ATP synthase activities in a mutant of the methanoarchaeon Methanothermobacter thermautotrophicus resistant to the protonophoric uncoupler TCS (3,3',4',5-tetrachlorosalicylanilide), the composition of membrane associated proteins from the wild-type and mutant strains has been compared. The uncoupler-resistance in the mutant strain was not accompanied by changes in a protein size or changes in the level of subunits A, B and c (proteolipid) of the A1A0-type ATPase-synthase. On the other hand, we revealed a 670-kDa membrane-associated protein complex that is abundantly present only in the mutant strain; it is composed of at least 5 different subunits of 95, 52, 42, 29 and 22 kDa.

References

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Apr 16, 1998·Biochimica Et Biophysica Acta·V P Skulachev
Mar 27, 2004·FEMS Microbiology Letters·L'ubomíra CubonováPeter Smigán

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