LptM promotes oxidative maturation of the lipopolysaccharide translocon by substrate binding mimicry

Yiying Yang, Haoxiang Chen, Robin A. Corey, Violette Morales, Yves Quentin, Carine Froment, Anne Caumont-Sarcos, Cécile Albenne, Odile Burlet-Schiltz, David Ranava, Phillip J. Stansfeld, Julien Marcoux and Raffaele Ieva ()
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Yiying Yang: Université de Toulouse, CNRS, Université Toulouse III - Paul Sabatier (UT3)
Haoxiang Chen: Université de Toulouse, CNRS, Université Toulouse III - Paul Sabatier (UT3)
Robin A. Corey: University of Oxford
Violette Morales: Université de Toulouse, CNRS, Université Toulouse III - Paul Sabatier (UT3)
Yves Quentin: Université de Toulouse, CNRS, Université Toulouse III - Paul Sabatier (UT3)
Carine Froment: Université de Toulouse, CNRS, Université Toulouse III - Paul Sabatier (UT3)
Anne Caumont-Sarcos: Université de Toulouse, CNRS, Université Toulouse III - Paul Sabatier (UT3)
Cécile Albenne: Université de Toulouse, CNRS, Université Toulouse III - Paul Sabatier (UT3)
Odile Burlet-Schiltz: Université de Toulouse, CNRS, Université Toulouse III - Paul Sabatier (UT3)
David Ranava: Université de Toulouse, CNRS, Université Toulouse III - Paul Sabatier (UT3)
Phillip J. Stansfeld: The University of Warwick
Julien Marcoux: Université de Toulouse, CNRS, Université Toulouse III - Paul Sabatier (UT3)
Raffaele Ieva: Université de Toulouse, CNRS, Université Toulouse III - Paul Sabatier (UT3)

Nature Communications, 2023, vol. 14, issue 1, 1-15

Abstract: Abstract Insertion of lipopolysaccharide (LPS) into the bacterial outer membrane (OM) is mediated by a druggable OM translocon consisting of a β-barrel membrane protein, LptD, and a lipoprotein, LptE. The β-barrel assembly machinery (BAM) assembles LptD together with LptE at the OM. In the enterobacterium Escherichia coli, formation of two native disulfide bonds in LptD controls translocon activation. Here we report the discovery of LptM (formerly YifL), a lipoprotein conserved in Enterobacteriaceae, that assembles together with LptD and LptE at the BAM complex. LptM stabilizes a conformation of LptD that can efficiently acquire native disulfide bonds, whereas its inactivation makes disulfide bond isomerization by DsbC become essential for viability. Our structural prediction and biochemical analyses indicate that LptM binds to sites in both LptD and LptE that are proposed to coordinate LPS insertion into the OM. These results suggest that, by mimicking LPS binding, LptM facilitates oxidative maturation of LptD, thereby activating the LPS translocon.

Date: 2023
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DOI: 10.1038/s41467-023-42007-w

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