Abstract：
:Pseudomonas aeruginosa ATCC 27853 and Pseudomonas sp. 593 use the phosphatidylcholine synthase pathway (Pcs-pathway) for the biosynthesis of phosphatidylcholine (PC). Both bacterial strains contain the phoA and lapA genes encoding alkaline phosphatases (ALP) and display strong ALP activities. The PhoA and LapA enzymes are thought to be independently secreted via the Xcp and Hxc type II secretion system (T2SS) subtypes, in which the Hxc system may act as a complementary mechanism when the Xcp pathway becomes limiting. Inactivation of the pcs gene in both bacteria abolished PC synthesis and resulted in approximately 50% less ALP activity in the cell-free culture. Analysis by western blotting showed that LapA protein content in the wild type and the pcs- mutant was unchanged in the cytoplasmic, periplasmic or extracellular protein fractions. In contrast, the PhoA protein in the pcs- mutant was less prevalent among extracellular proteins but was more abundant in the periplasmic protein fraction compared to the wild type. Semi- quantitative reverse transcriptase PCR showed that phoA, lapA and 12 xcp genes were equally expressed at the transcriptional level in both the wild types and the pcs- mutants. Our results demonstrate that the absence of PC in bacterial membrane phospholipids does not interfere with the transcription of the phoA and lapA genes but primarily affects the export of PhoA from the cytoplasm to the extracellular environment via the Xcp T2SS.
journal_name
Microbiol Resjournal_title
Microbiological researchauthors
Liu X,Long D,You H,Yang D,Zhou S,Zhang S,Li M,He M,Xiong M,Wang Xdoi
10.1016/j.micres.2016.02.001subject
Has Abstractpub_date
2016-11-01 00:00:00pages
21-29eissn
0944-5013issn
1618-0623pii
S0944-5013(16)30006-4journal_volume
192pub_type
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