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Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein.

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  • 1. Unité de Génétique Moléculaire, CNRS URA 1149, Institut Pasteur, Paris, France.
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    • Hardie KR 1
    (1 author)

ORCIDs linked to this article

The EMBO Journal, 01 Mar 1996, 15(5):978-988
https://doi.org/10.1002/j.1460-2075.1996.tb00434.x PMID: 8605893 PMCID: PMC449992

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Abstract 

Only one of the characterized components of the main terminal branch of the general secretory pathway (GSP) in Gram-negative bacteria, GspD, is an integral outer membrane protein that could conceivably form a channel to permit protein transport across this membrane. PulD, a member of the GspD protein family required for pullulanase secretion by Klebsiella oxytoca, is shown here to form outer membrane-associated complexes which are not readily dissociated by SDS treatment. The outer membrane association of PulD is absolutely dependent on another component of the GSP, the outer membrane-anchored lipoprotein PulS. Furthermore, the absence of PulS resulted in limited proteolysis of PulD and caused induction of the so-called phage shock response, as measured by increased expression of the pspA gene. We propose that PulS may be the first member of a new family of periplasmic chaperones that are specifically required for the insertion of a group of outer membrane proteins into this membrane. PulS is only the second component of the main terminal branch of the GSP for which a precise function can be proposed.

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EMBO J. 1996 Mar 1; 15(5): 978–988.
PMCID: PMC449992
PMID: 8605893

Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein.

K R Hardie, S Lory, and A P Pugsley
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Abstract

Only one of the characterized components of the main terminal branch of the general secretory pathway (GSP) in Gram-negative bacteria, GspD, is an integral outer membrane protein that could conceivably form a channel to permit protein transport across this membrane. PulD, a member of the GspD protein family required for pullulanase secretion by Klebsiella oxytoca, is shown here to form outer membrane-associated complexes which are not readily dissociated by SDS treatment. The outer membrane association of PulD is absolutely dependent on another component of the GSP, the outer membrane-anchored lipoprotein PulS. Furthermore, the absence of PulS resulted in limited proteolysis of PulD and caused induction of the so-called phage shock response, as measured by increased expression of the pspA gene. We propose that PulS may be the first member of a new family of periplasmic chaperones that are specifically required for the insertion of a group of outer membrane proteins into this membrane. PulS is only the second component of the main terminal branch of the GSP for which a precise function can be proposed.

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Selected References

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