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A coiled-coil domain triggers oligomerization of MmpL10, the mycobacterial transporter of trehalose polyphleate precursor

Couston, Julie ; Feuillard, Jérôme ; Ancelin, Aurélie ; Lai-Kee-Him, Joséphine ; Brodolin, Konstantin ; Chalut, Christian ; Gourdon, Pontus LU and Blaise, Mickaël (2025) In FEBS Letters 599(12). p.1682-1697
Abstract

The mycobacterial outer membrane is composed of unusual lipids and glycolipids. Some of these lipids are exported to the cell envelope by resistance-nodulation-division (RND) transporters called mycobacterial membrane protein large (MmpL). While the oligomeric state of most RND transporters is well established, MmpL assembly remains unclear. Here, we investigated MmpL10, the trehalose polyphleate transporter. Biochemical data suggest that MmpL10 forms a homotrimer and that its oligomerization is driven by a coiled-coil domain. Structural modeling and electron microscopy data reveal the presence of a tubular extension that spans the mycobacterial cell wall and reaches the mycomembrane. As most MmpL proteins possess this extension,... (More)

The mycobacterial outer membrane is composed of unusual lipids and glycolipids. Some of these lipids are exported to the cell envelope by resistance-nodulation-division (RND) transporters called mycobacterial membrane protein large (MmpL). While the oligomeric state of most RND transporters is well established, MmpL assembly remains unclear. Here, we investigated MmpL10, the trehalose polyphleate transporter. Biochemical data suggest that MmpL10 forms a homotrimer and that its oligomerization is driven by a coiled-coil domain. Structural modeling and electron microscopy data reveal the presence of a tubular extension that spans the mycobacterial cell wall and reaches the mycomembrane. As most MmpL proteins possess this extension, oligomerization may be a common feature of this family of transporters, possibly involved in the transport of the MmpL cargo.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
coiled-coil, MmpL, mycobacteria, Mycobacterium smegmatis, RND transporter, TPP
in
FEBS Letters
volume
599
issue
12
pages
16 pages
publisher
Wiley-Blackwell
external identifiers
  • scopus:105007648989
  • pmid:40468558
ISSN
0014-5793
DOI
10.1002/1873-3468.70085
language
English
LU publication?
yes
additional info
Publisher Copyright: © 2025 The Author(s). FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
id
faf9dc7a-e94e-4fe9-8dbb-1931996b6908
date added to LUP
2025-12-30 15:22:08
date last changed
2026-02-24 20:16:56
@article{faf9dc7a-e94e-4fe9-8dbb-1931996b6908,
  abstract     = {{<p>The mycobacterial outer membrane is composed of unusual lipids and glycolipids. Some of these lipids are exported to the cell envelope by resistance-nodulation-division (RND) transporters called mycobacterial membrane protein large (MmpL). While the oligomeric state of most RND transporters is well established, MmpL assembly remains unclear. Here, we investigated MmpL10, the trehalose polyphleate transporter. Biochemical data suggest that MmpL10 forms a homotrimer and that its oligomerization is driven by a coiled-coil domain. Structural modeling and electron microscopy data reveal the presence of a tubular extension that spans the mycobacterial cell wall and reaches the mycomembrane. As most MmpL proteins possess this extension, oligomerization may be a common feature of this family of transporters, possibly involved in the transport of the MmpL cargo.</p>}},
  author       = {{Couston, Julie and Feuillard, Jérôme and Ancelin, Aurélie and Lai-Kee-Him, Joséphine and Brodolin, Konstantin and Chalut, Christian and Gourdon, Pontus and Blaise, Mickaël}},
  issn         = {{0014-5793}},
  keywords     = {{coiled-coil; MmpL; mycobacteria; Mycobacterium smegmatis; RND transporter; TPP}},
  language     = {{eng}},
  number       = {{12}},
  pages        = {{1682--1697}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{FEBS Letters}},
  title        = {{A coiled-coil domain triggers oligomerization of MmpL10, the mycobacterial transporter of trehalose polyphleate precursor}},
  url          = {{http://dx.doi.org/10.1002/1873-3468.70085}},
  doi          = {{10.1002/1873-3468.70085}},
  volume       = {{599}},
  year         = {{2025}},
}