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Depletion of phosphatidylethanolamine affects secretion of Escherichia coli alkaline phosphatase and its transcriptional expression
Author(s) -
Mikhaleva Natalia I,
Golovastov Victor V,
Zolov Sergey N,
Bogdanov Mikhail V,
Dowhan William,
Nesmeyanova Marina A
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02288-8
Subject(s) - phosphatidylethanolamine , phospholipid , regulon , cardiolipin , escherichia coli , alkaline phosphatase , secretion , phosphatase , biochemistry , phosphatidylinositol , chemistry , microbiology and biotechnology , biology , phosphatidylcholine , membrane , signal transduction , enzyme , gene
In this report we demonstrate that depletion of the major phospholipid phosphatidylethanolamine, a single non‐bilayer forming phospholipid of Escherichia coli , significantly reduces the secretion efficiency of alkaline phosphatase in vivo. Secretion, however, is correlated with the content in membranes of cardiolipin, which in combination with selected divalent cations has a strong tendency to adopt a non‐bilayer state indicating the possible involvement of lipid polymorphism in efficient protein secretion. Depletion of this zwitterionic phospholipid also inhibits expression of the protein controlled by the endogenous P PHO promoter but not the P BAD promoter, which is suggested to be due to the effect of unbalanced phospholipid composition on the orthophosphate signal transduction system (Pho regulon) through an effect on its membrane bound sensor.