Molecular and biochemical characterization of mechanosensitive channels in Corynebacterium glutamicum.
Database searches in the Corynebacterium glutamicum genome sequence revealed homologs of the mechanosensitive channels MscL and YggB of Escherichia coli. To elucidate the physiological role of these putative channels deletion mutants were constructed. Betaine efflux induced by osmotic downshock of the mscL deletion mutant was nearly identical to that of the wild-type, whereas the yggB deletion mutant showed a reduced efflux rate. Interestingly, the double deletion strain, which was expected to have an even more decreased capability of betaine excretion, had only a slightly reduced efflux rate compared to the wild-type and did not show an increased mortality after osmotic downshift. These results led to the hypothesis that C. glutamicum may possess a third type of mechanosensitive channel not related to the MscL and YggB/KefA families. Furthermore it is unlikely that an MscM-like activity is responsible for the betaine efflux, because of the high transport capacity detected in the double deletion mutant.
Nottebrock
Daniel
D
Institut für Biochemie, Universität Köln, Zülpicher Str. 47, D-50674, Köln, Germany.
Meyer
Ute
U
Krämer
Reinhard
R
Morbach
Susanne
S
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D001622:Betaine / Q000032:analysis / Q000378:metabolism; D001692:Biological Transport; D003352:Corynebacterium / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003470:Culture Media; D004926:Escherichia coli / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D016366:Open Reading Frames; D009997:Osmotic Pressure
D001426:Bacterial Proteins; D003470:Culture Media; D026901:Membrane Transport Proteins; D001622:Betaine