Three putative cation/proton antiporters from the soda lake alkaliphile Alkalimonas amylolytica N10 complement an alkali-sensitive Escherichia coli mutant
نویسندگان
چکیده
منابع مشابه
The activity profile of the NhaD-type Na+(Li+)/H+ antiporter from the soda Lake Haloalkaliphile Alkalimonas amylolytica is adaptive for the extreme environment.
In extreme alkaliphiles, Na(+)/H(+) antiporters play a central role in the Na(+) cycle that supports pH homeostasis, Na(+) resistance, solute uptake, and motility. Properties of individual antiporters have only been examined in extremely alkaliphilic soil Bacillus spp., whereas the most alkaline natural habitats usually couple high pH with high salinity. Here, studies were conducted on a Na(+)(...
متن کاملFurther characterization of a complement-sensitive mutant of a virulent avian Escherichia coli isolate.
An attempt was made to characterize the mechanism of complement resistance operating in a virulent avian Escherichia coli isolate. Using flow cytometry to detect antibody to C3, we found that there was significantly more antibody bound to a complement-sensitive mutant of this wild type than to the parent organism, suggesting that more C3 subunits were bound to the wild type. Neither the wild ty...
متن کاملGas channels for NH(3): proteins from hyperthermophiles complement an Escherichia coli mutant.
Ammonium transport (Amt) proteins appear to be bidirectional channels for NH(3). The amt genes of the hyperthermophiles Aquifex aeolicus and Methanococcus jannaschii complement enteric amtB mutants for growth at 25 nM NH(3) at 37 degrees C. To our knowledge, Amt proteins are the first hyperthermophilic membrane transport proteins shown to be active in a mesophilic bacterium. Despite low express...
متن کاملFormation of transmural complement pores in serum-sensitive Escherichia coli.
The binding of C9 at 0 and 37 degrees C to viable Escherichia coli K-12 cells carrying C5b-8 complexes was quantified. At low temperature, limited average binding of only 1 to 1.4 molecules of C9 per C8 molecule occurred, whereas 6 to 8 C9 molecules were bound per C8 molecule at 37 degrees C. Despite incorporation of C9 into C5b-9 complexes at 0 degrees C, these terminal complexes caused no los...
متن کاملA mutant of Escherichia coli with temperature-sensitive streptomycin protein.
The temperature-sensitive mutation in our Escherichia coli strain C1714 appears to be in a ribosomal protein. The mutation maps at the streptomycin locus. Protein synthesis in intact cells stops immediately when the temperature is shifted from 30 to 42 degrees C. Analysis of polyribosome distributions after shift-up suggests that initiation of protein synthesis is defective at the high temperat...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Microbiology
سال: 2007
ISSN: 1350-0872,1465-2080
DOI: 10.1099/mic.0.2007/007450-0