Depletion of phosphatidylethanolamine affects secretion of Escherichia coli alkaline phosphatase and its transcriptional expression

FEBS Letters

Dowhan, William¹  Golovastov, Victor V²  Bogdanov, Mikhail V¹  Mikhaleva, Natalia I²  Zolov, Sergey N²  Nesmeyanova, Marina A² 

[1] Department of Biochemistry and Molecular Biology, University of Texas-Houston, Medical School, Houston, TX 77030, USA;Laboratory of Protein Secretion in Bacteria, Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia

关键词: Alkaline phosphatase;    Protein expression;    Protein translocation;    Phosphatidylethanolamine;    Pho regulon;    Escherichia coli;    PhoA and prePhoA;    Escherichia coli alkaline phosphatase and its precursor;    respectively;    PE;    phosphatidylethanolamine;    CL;    cardiolipin;    Pi;    orthophosphate;    TCA;    trichloroacetic acid;    SDS–PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(01)02288-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown