Amiloride resistance in the methanoarcheon Methanothermobacter thermoautotrophicus: characterization of membrane-associated proteins
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
17007434
DOI
10.1007/bf02931822
Knihovny.cz E-resources
- MeSH
- Amiloride pharmacology MeSH
- Drug Resistance, Bacterial drug effects genetics physiology MeSH
- Bacterial Proteins chemistry drug effects MeSH
- Sodium Channel Blockers pharmacology MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Membrane Proteins chemistry drug effects genetics MeSH
- Methanobacteriaceae drug effects genetics physiology MeSH
- Mutant Proteins chemistry drug effects MeSH
- Sodium-Hydrogen Exchangers chemistry drug effects MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization methods MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Amiloride MeSH
- Bacterial Proteins MeSH
- Sodium Channel Blockers MeSH
- Membrane Proteins MeSH
- Mutant Proteins MeSH
- Sodium-Hydrogen Exchangers MeSH
An amiloride-resistant mutant with diminished Na+/H+ antiporter activity was isolated from Methanothermobacter thermoautotrophicus. To define the protein basis of amiloride resistance, the composition of membrane-associated proteins was partially characterized and compared with that of the wild type strain. An abundant 670-kDa membrane-associated protein that was present only in the mutant strain was analyzed by MALDI-TOF MS and identified as a coenzyme F420-reducing hydrogenase. The amiloride resistance was not accompanied by changes in protein size or changes in the level of subunits A or B of the A1A0-type ATP synthase; on the other hand, the SDS-PAGE patterns of the chloroform-methanol extract of membranes from both strains were different. Two bands with calculated molecular mass 16 and 11 kDa were identified as MtrD and AtpK, respectively. The observed over-expression of a 22.7-kDa protein in the mutant cells may represent the multimeric form of the MtrD subunit. These results show that the impairment of the Na+/H+ antiporter system in the amiloride-resistant mutant of Methanothermobacter thermoautotrophicus is accompanied by only small changes in a few membrane-associated proteins.
See more in PubMed
Nature. 1970 Aug 15;227(5259):680-5 PubMed
J Bacteriol. 1998 Jul;180(13):3448-52 PubMed
Folia Microbiol (Praha). 2004;49(5):519-25 PubMed
FEBS Lett. 1997 Dec 22;420(1):93-6 PubMed
Folia Microbiol (Praha). 2004;49(2):147-50 PubMed
Biochem Mol Biol Int. 1997 Sep;43(1):123-32 PubMed
FEBS Lett. 1998 Mar 27;425(2):204-8 PubMed
FEMS Microbiol Lett. 2001 Feb 5;195(1):47-51 PubMed
Eur J Biochem. 1989 Dec 8;186(1-2):309-16 PubMed
J Bioenerg Biomembr. 1989 Dec;21(6):635-47 PubMed
Biochim Biophys Acta. 1994 Apr 28;1185(2):129-51 PubMed
Distinctive archaebacterial species associated with anaerobic rumen protozoan Entodinium caudatum
