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Secretion of Serratia liquefaciens phospholipase from Escherichia coli
Author(s) -
Givskov Michael,
Molin Søren
Publication year - 1993
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1993.tb01567.x
Subject(s) - biology , operon , regulon , secretion , escherichia coli , phospholipase , microbiology and biotechnology , serratia marcescens , chemotaxis , phospholipase d , phospholipase c , biochemistry , gene , enzyme , receptor
Summary The Serratia liquefaciens phospholipase (PhIA) is secreted to the medium from its natural host. Here we present results which indicate that, when cloned and expressed in Escherichia coli , secretion can be mediated by a putative host‐encoded pathway, expression of which is controlled by FlhD (formerly FlbB), the master regulator of the flagellar/ chemotaxis regulon. In the absence of this secretion pathway, the synthesized phospholipase accumulates inside the host cell where it forms a complex with the PhlB protein. PhlB, which is encoded from the promoter distal gene of the phospholipase operon, inhibits the phospholipase activity of PhlA. Formation of this enzymatically inactive PhlA/PhlB complex is required for maintenance of cell viability.