Kawamoto et al. (2009) suggested recently that EPA affects

the synthesis of some membrane proteins at a low temperature (4 °C) in the cold-adapted bacterium Shewanella livingstonensis Ac10 because the protein levels decreased in the EPA-deficient mutants of this strain. One such protein (Omp_C176) is inducibly produced in parental cells at 4 °C (Kawamoto et al., 2007). It was suggested that the stability of Omp_C176 and other outer membrane proteins at a low temperature depends on EPA-containing phospholipids and that such proteins facilitate the ERK inhibitor membrane passage of hydrophilic nutrients through porin (Kawamoto et al., 2009). However, this would not be applicable to IK-1 for the following reasons. First, IK-1 and IK-1Δ8 were cultivated at 20 °C in this study. Second, the effects on the stability and abundance of porin proteins such as Omp_C176, which should accelerate the entry of both nutrients and growth inhibitors with a molecular weight less http://www.selleckchem.com/products/bay80-6946.html than about 600 into cells possessing EPA and thereby induce greater resistance to antibiotics in IK-1 cells with EPA than in IK-1Δ8 with no EPA, are controversial. Third, an E. coli recombinant with EPA grown at 20 °C was also more resistant to water-soluble

antibiotics than was the control E. coli recombinant with no EPA (R. Hori, T. Nishida & H. Okuyama, unpublished data). One principal strategy for bacterial survival against drugs such as antibiotics is an ability to pump these compounds out of the cell (Walsh, 2000; Martinez et al., 2009). Although we have no biochemical or molecular evidence, it is possible that EPA (and other polyunsaturated fatty acids) increases the activity of membrane efflux pumps in EPA-producing bacteria; the synthesis of some porin proteins is accelerated in EPA-producing S. livingstonensis heptaminol Ac10 (Kawamoto et al., 2009). Interestingly, a group of proteins whose concentrations

are decreased by EPA depletion in the mutant of S. livingstonensis Ac10 include a tentative TolC family protein. It is known that TolC is involved in the efflux of enterobactin (Bleuel et al., 2005) and various types of drugs (Nikaido, 1996; Blair & Piddock, 2009) across the outer membrane in E. coli. Therefore, EPA may affect the synthesis of some efflux proteins or protein structures, irrespective of the temperature. According to Andersen & Koeppe (2007), the lipid bilayer thickness correlates with membrane protein functions. Interestingly, polyunsaturated fatty acids such as DHA, EPA, and arachidonic acid may modulate membrane protein functions, including various channel and enzyme activities, through bilayer-mediated mechanisms that do not involve specific protein binding, but rather changes in bilayer material properties (e.g. thickness, curvature, elastic compression, and bending modulus) in prokaryotic and eukaryotic systems.