S1, significantly more PAO1 cells adhered to lung cells compared to the PAO1Δ2950. Strain PAO1Δ2950 complemented with a plasmid pDN18 encoding pfm (strain Δ2950C) recovered much of the lost adherence. Furthermore, we also detected C4-HSL and 3O-C12-HSL of the PAO1 and the PAO1Δ2950 by E. coli DH5α(pECP61.5, rhlA’-lacZ) and E. coli DH5α(pECP64, lasB’-lacZ), respectively, and the PAO1Δ2950 displayed similar defect Daporinad as I69 in the QS system (data not shown), demonstrating that the influence of pfm on the bacterial adherence and QS is not a strain-specific
phenomenon. In conclusion, pfm affected the adherence of P. aeruginosa and the synthesis of QS signals C4-HSL and 3O-C12-HSL which had no effect on the swimming mobility Dabrafenib in vitro of P. aeruginosa (Reimmann et al., 2002). As the QS system was shown to influence the adherence of P. aeruginosa, our results suggested that PFM might regulate the adherence of P. aeruginosa via controlling the QS system. Considering that PFM and FabI have been reported to be involved in the biosynthesis of fatty acids (Zhu et al., 2010), we believed that pfm might be involved in energy metabolism which supplies energy for bacterial swimming. On the other hand, pfm affected the production of acyl groups which provided acyl groups supporting
the synthesis of AHLs. However, knockout of pfm did not eliminate the generation of AHLs, possibly because the fabI gene product also supports the synthesis of AHLs. Unfortunately, deletion of both fabI and pfm seems to be lethal as we tried multiple times to obtain the double mutant without success. Thus, it should be plausible to obtain a conditional double knockout mutant to uncover their roles in the pathology of P. aeruginosa Cobimetinib chemical structure in the future. This project was supported in part by National Basic Research Program of China (973 Program, 2012CB518700). We thank Yuehe
Ding (National Institute of Biological Sciences, Beijing, China) and Zhihong Wang (Nankai University, Tianjin, China) for their assistants in carrying out experiments and Dr Barbara H. Iglewski (University of Rochester, USA) for providing biosensors pECP64 and pECP61.5. “
“The Gram-positive soil bacterium Bacillus subtilis uses glucose and malate as the preferred carbon sources. In the presence of either glucose or malate, the expression of genes and operons for the utilization of secondary carbon sources is subject to carbon catabolite repression. While glucose is a preferred substrate in many organisms from bacteria to man, the factors that contribute to the preference for malate have so far remained elusive. In this work, we have studied the contribution of the different malate-metabolizing enzymes in B. subtilis, and we have elucidated their distinct functions. The malate dehydrogenase and the phosphoenolpyruvate carboxykinase are both essential for malate utilization; they introduce malate into gluconeogenesis.