Back to Search
Start Over
Osmosensing and osmosignaling in Corynebacterium glutamicum.
- Source :
-
Amino acids [Amino Acids] 2009 Sep; Vol. 37 (3), pp. 487-97. Date of Electronic Publication: 2009 Mar 24. - Publication Year :
- 2009
-
Abstract
- The Gram-positive soil bacterium Corynebacterium glutamicum is used in microbial biotechnology for the large-scale production of amino acids, e.g., L: -glutamate and L: -lysine. We have studied the response of this organism to hyperosmotic challenge at the level of both transcription and protein activity. Two systems responding to hyperosmotic stress in C. glutamicum are reviewed here, the two component system MtrAB and the glycine-betaine uptake system BetP. The osmosensory two-component system consists of the membrane-bound histidine kinase MtrB and the soluble response regulator MtrA. MtrB was shown to perceive a so far unknown physical stimulus related to hyperosmotic stress via the cytoplasmically oriented phosphorylation domain, and to transduce the signal to the DNA via MtrA. The secondary active transporter BetP takes up betaine in cotransport with two Na(+) ions. BetP responds to hyperosmotic stress by increased transcription mediated via MtrAB signaling, and by instant activation of transport. In the mechanism of BetP activation, the C-terminal, regulatory domain of BetP, the cytoplasmic concentration of K(+), and negative membrane surface charges are involved. The molecular mechanism of the activation process is discussed in relation to the recently published X-ray structure of BetP.
- Subjects :
- ATP-Binding Cassette Transporters physiology
Bacterial Proteins genetics
Carrier Proteins physiology
Cell Membrane physiology
Models, Biological
Osmolar Concentration
Osmotic Pressure physiology
RNA-Binding Proteins genetics
RNA-Binding Proteins physiology
Symporters
Transcription Factors genetics
Transcription Factors physiology
Bacterial Proteins physiology
Corynebacterium glutamicum physiology
Signal Transduction physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1438-2199
- Volume :
- 37
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Amino acids
- Publication Type :
- Academic Journal
- Accession number :
- 19308662
- Full Text :
- https://doi.org/10.1007/s00726-009-0271-6