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EMBO J. 1996 Mar 1;15(5):978-88.

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

Author information

1
Unité de Génétique Moléculaire, CNRS URA 1149, Institut Pasteur, Paris, France.

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.

PMID:
8605893
PMCID:
PMC449992
[Indexed for MEDLINE]
Free PMC Article

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