| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Previous Article | Next Article ![]()
Institut für Biochemie der Universität zu Köln, Zülpicher Str. 47, 50674 Köln, Germany; Institut für Mikrobiologie und Weinforschung, Johannes Gutenberg-Universität Mainz, Becherweg 15, 55099 Mainz, Germany
* To whom correspondence should be addressed. Email:
s.morbach{at}uni-koeln.de.
The two-component system MtrBA is involved in the osmostress response of Corynebacterium glutamicum. MtrB was reconstituted in functionally active form in liposomes and showed autophosphorylation and phosphatase activity. In proteoliposomes MtrB activity was stimulated by monovalent cations used by many osmosensors for detection of hypertonicity. Although MtrB was activated by monovalent cations they lead in vitro to a general stabilization of histidine kinases, and do not represent the stimulus for MtrB to sense hyperosmotic stress.
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.
In vitro analysis of the two-component system MtrB-MtrA from Corynebacterium glutamicum
![]()
Abstract
This article has been cited by other articles:
| Appl. Environ. Microbiol. | Infect. Immun. | Eukaryot. Cell |
|---|---|---|
| Mol. Cell. Biol. | J. Virol. | Microbiol. Mol. Biol. Rev. |
| ALL ASM JOURNALS |