| Literature DB >> 10781562 |
A F Elias1, J L Bono, J A Carroll, P Stewart, K Tilly, P Rosa.
Abstract
The homolog of the chromosomally encoded stationary-phase sigma factor RpoS in Borrelia burgdorferi was inactivated using gyrB(r) as a selectable marker. Two-dimensional nonequilibrium pH gradient electrophoresis of stationary-phase cell lysates identified at least 11 differences between the protein profiles of the rpoS mutant and wild-type organisms. Wild-type B. burgdorferi had a growth phase-dependent resistance to 1 N NaCl, similar to the stationary-phase response reported for other bacteria. The B. burgdorferi rpoS mutant strain was less resistant to osmotic stress in stationary phase than the isogenic rpoS wild-type organism. The results indicate that the B. burgdorferi rpoS homolog influences protein composition and participates in stationary-phase-dependent osmotic resistance. This rpoS mutant will be useful for studying regulation of gene expression in response to changing environmental conditions.Entities:
Mesh:
Substances:
Year: 2000 PMID: 10781562 PMCID: PMC102002 DOI: 10.1128/JB.182.10.2909-2918.2000
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490