Journal
JOURNAL OF BACTERIOLOGY
Volume 185, Issue 19, Pages 5901-5905Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.185.19.5901-5905.2003
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Funding
- FIC NIH HHS [TW05645, F06 TW005645] Funding Source: Medline
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The OmpD porin is the most abundant outer membrane protein in Salmonella enterica serovar Typhimurium and represents about 1% of total cell protein. Unlike the case with the less abundant OmpC and OmpF porins, the stoichiometry of OmpD in the outer membrane does not change in response to changes in osmolarity. The abundance of OmpD increases in response to anaerobiosis and decreases in response to low pH, conditions encountered by serovar Typhimurium during the infection of its murine host. By constructing an operon fusion of the lacZY genes with the ompD promoter, we show that the abundance of OmpD in the outer membrane is regulated primarily at the level of transcription and is subject to catabolite repression. In response to anaerobiosis, the abundance of OmpD in the outer membrane also appears to be controlled posttranscriptionally by a function dependent on Fnr.
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