Secretion of Serratia liquefaciens phospholipase from Escherichia coli

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Secretion of Serratia liquefaciens phospholipase from Escherichia coli. / Givskov, M; Molin, Søren.

In: Molecular Microbiology, Vol. 8, No. 2, 1993, p. 229-42.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Givskov, M & Molin, S 1993, 'Secretion of Serratia liquefaciens phospholipase from Escherichia coli', Molecular Microbiology, vol. 8, no. 2, pp. 229-42.

APA

Givskov, M., & Molin, S. (1993). Secretion of Serratia liquefaciens phospholipase from Escherichia coli. Molecular Microbiology, 8(2), 229-42.

Vancouver

Givskov M, Molin S. Secretion of Serratia liquefaciens phospholipase from Escherichia coli. Molecular Microbiology. 1993;8(2):229-42.

Author

Givskov, M ; Molin, Søren. / Secretion of Serratia liquefaciens phospholipase from Escherichia coli. In: Molecular Microbiology. 1993 ; Vol. 8, No. 2. pp. 229-42.

Bibtex

@article{b190d0d043654036a5125f84bb5077d0,
title = "Secretion of Serratia liquefaciens phospholipase from Escherichia coli",
abstract = "The Serratia liquefaciens phospholipase (PhlA) 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.",
author = "M Givskov and S{\o}ren Molin",
year = "1993",
language = "English",
volume = "8",
pages = "229--42",
journal = "Molecular Microbiology",
issn = "0950-382X",
publisher = "Wiley-Blackwell",
number = "2",

}

RIS

TY - JOUR

T1 - Secretion of Serratia liquefaciens phospholipase from Escherichia coli

AU - Givskov, M

AU - Molin, Søren

PY - 1993

Y1 - 1993

N2 - The Serratia liquefaciens phospholipase (PhlA) 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.

AB - The Serratia liquefaciens phospholipase (PhlA) 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.

M3 - Journal article

C2 - 8316077

VL - 8

SP - 229

EP - 242

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 2

ER -

ID: 44293771