Effects of linker insertions on the biogenesis and functioning of the Escherichia coli outer membrane pore protein PhoE

1987 ◽  
Vol 208 (3) ◽  
pp. 485-489 ◽  
Author(s):  
Dirk Bosch ◽  
Jan Tommassen
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Membrane Pore ◽  
Pore Protein

scholarly journals Characterization of the interfacial behavior and structure of the signal sequence of Escherichia coli outer membrane pore protein PhoE.

1988 ◽  
Vol 263 (9) ◽  
pp. 4202-4207 ◽  
Author(s):  
A M Batenburg ◽  
R Brasseur ◽  
J M Ruysschaert ◽  
G J van Scharrenburg ◽  
A J Slotboom ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Signal Sequence ◽  
Interfacial Behavior ◽  
Membrane Pore ◽  
Pore Protein

scholarly journals An Excretory Function for the Escherichia coli Outer Membrane Pore TolC: Upregulation of marA and soxS Transcription and Rob Activity Due to Metabolites Accumulated in tolC Mutants

2009 ◽  
Vol 191 (16) ◽  
pp. 5283-5292 ◽  
Author(s):  
Judah L. Rosner ◽  
Robert G. Martin
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Bile Salts ◽  
Efflux Pumps ◽  
Membrane Channel ◽  
Protein Activity ◽  
Membrane Pore ◽  
Excretory Function ◽  
Outer Membrane Channel ◽  
Transcriptional Fusions

ABSTRACT Efflux pumps function to rid bacteria of xenobiotics, including antibiotics, bile salts, and organic solvents. TolC, which forms an outer membrane channel, is an essential component of several efflux pumps in Escherichia coli. We asked whether TolC has a role during growth in the absence of xenobiotics. Because tolC transcription is activated by three paralogous activators, MarA, SoxS, and Rob, we examined the regulation of these activators in tolC mutants. Using transcriptional fusions, we detected significant upregulation of marRAB and soxS transcription and Rob protein activity in tolC mutants. Three mechanisms could be distinguished: (i) activation of marRAB transcription was independent of marRAB, soxR, and rob functions; (ii) activation of soxS transcription required SoxR, a sensor of oxidants; and (iii) Rob protein was activated posttranscriptionally. This mechanism is similar to the mechanisms of upregulation of marRAB, soxS, and Rob by treatment with certain phenolics, superoxides, and bile salts, respectively. The transcription of other marA/soxS/rob regulon promoters, including tolC itself, was also elevated in tolC mutants. We propose that TolC is involved in the efflux of certain cellular metabolites, not only xenobiotics. As these metabolites accumulate during growth, they trigger the upregulation of MarA, SoxS, and Rob, which in turn upregulate tolC and help rid the bacteria of these metabolites, thereby restoring homeostasis.

Gene encoding a hybrid OmpF-PhoE pore protein in the outer membrane of Escherichia coli K12

1984 ◽  
Vol 197 (3) ◽  
pp. 503-508 ◽  
Author(s):  
Jan Tommassen ◽  
Anthony P. Pugsley ◽  
Jaap Korteland ◽  
John Verbakel ◽  
Ben Lugtenberg
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Gene Encoding ◽  
Escherichia Coli K12 ◽  
Pore Protein

scholarly journals O-antigenic chains of lipopolysaccharide prevent binding of antibody molecules to an outer membrane pore protein in Enterobacteriaceae

1986 ◽  
Vol 1 (1) ◽  
pp. 43-49 ◽  
Author(s):  
Peter van der Ley ◽  
Oscar Kuipers ◽  
Jan Tommassen ◽  
Ben Lugtenberg
Keyword(s):  
Outer Membrane ◽  
Membrane Pore ◽  
Pore Protein

Cloning of ompF, the structural gene for an outer membrane pore protein of E. coli K12: Physical localization and homology with the phoE gene

1982 ◽  
Vol 185 (1) ◽  
pp. 105-110 ◽  
Author(s):  
Jan Tommassen ◽  
Peter van der Ley ◽  
Arie van der Ende ◽  
Hans Bergmans ◽  
Ben Lugtenberg
Keyword(s):  
Outer Membrane ◽  
Structural Gene ◽  
Membrane Pore ◽  
E Coli ◽  
Pore Protein
Sign in / Sign up

Export Citation Format

Share Document