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The Stable Interaction Between Signal Peptidase LepB of Escherichia coli and Nuclease Bacteriocins Promotes Toxin Entry into the Cytoplasm.

By Liliana Mora, Karine Moncoq, Patrick England, Jacques Oberto and Miklos de Zamaroczy

Abstract

International audienceLepB is a key membrane component of the cellular secretion machinery, which releases secreted proteins into the periplasm by cleaving the inner membrane-bound leader. We showed that LepB is also an essential component of the machinery hijacked by the tRNase colicin D for its import. Here we demonstrate that this non-catalytic activity of LepB is to promote the association of the central domain of colicin D with the inner membrane before the FtsH-dependent proteolytic processing and translocation of the toxic tRNase domain into the cytoplasm. The novel structural role of LepB results in a stable interaction with colicin D, with a stoichiometry of 1:1 and a nanomolar Kd determined in vitro. LepB provides a chaperone-like function for the penetration of several nuclease-type bacteriocins into target cells. The colicin-LepB interaction is shown to require only a short peptide sequence within the central domain of these bacteriocins and to involve residues present in the short C-terminal Box E of LepB. Genomic screening identified the conserved LepB binding motif in colicin-like ORFs from 13 additional bacterial species. These findings establish a new paradigm for the functional adaptability of an essential inner-membrane enzyme

Topics: toxicity, endonuclease, colicin, bacteriocin, LepB, protease, protein import, membrane, microbiology, [ SDV ] Life Sciences [q-bio]
Publisher: American Society for Biochemistry and Molecular Biology
Year: 2015
DOI identifier: 10.1074/jbc.M115.691907
OAI identifier: oai:HAL:hal-01430012v1
Provided by: Hal-Diderot
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