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The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism

The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism
The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism

Coordination of outer membrane constriction with septation is critical to faithful division in Gram-negative bacteria and vital to the barrier function of the membrane. This coordination requires the recruitment of the peptidoglycan-binding outer-membrane lipoprotein Pal at division sites by the Tol system. Here, we show that Pal accumulation at Escherichia coli division sites is a consequence of three key functions of the Tol system. First, Tol mobilises Pal molecules in dividing cells, which otherwise diffuse very slowly due to their binding of the cell wall. Second, Tol actively captures mobilised Pal molecules and deposits them at the division septum. Third, the active capture mechanism is analogous to that used by the inner membrane protein TonB to dislodge the plug domains of outer membrane TonB-dependent nutrient transporters. We conclude that outer membrane constriction is coordinated with cell division by active mobilisation-and-capture of Pal at division septa by the Tol system.

2041-1723
Szczepaniak, Joanna
099f91d3-1203-46f7-9bdc-53ab04e82c69
Holmes, Peter
a4df8275-8f6e-4f55-b5a4-cef39ec4bbfa
Rajasekar, Karthik
80c0f9c0-4e24-4f23-aefe-6e2542fad2da
Kaminska, Renata
b98fd406-e88c-475d-a573-d6b2810c86d9
Samsudin, Firdaus
b01e87a0-af50-44d6-bca4-f511c40165f9
Inns, Patrick George
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Rassam, Patrice
2516d2de-abe9-4b88-b69a-7fa5bba29787
Khalid, Syma
90fbd954-7248-4f47-9525-4d6af9636394
Murray, Seán M.
8c6aefa5-dc51-4926-898c-859d733e8f50
Redfield, Christina
870a366a-9440-4f60-bf2a-ac8e8e864c29
Kleanthous, Colin
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Szczepaniak, Joanna
099f91d3-1203-46f7-9bdc-53ab04e82c69
Holmes, Peter
a4df8275-8f6e-4f55-b5a4-cef39ec4bbfa
Rajasekar, Karthik
80c0f9c0-4e24-4f23-aefe-6e2542fad2da
Kaminska, Renata
b98fd406-e88c-475d-a573-d6b2810c86d9
Samsudin, Firdaus
b01e87a0-af50-44d6-bca4-f511c40165f9
Inns, Patrick George
7fdcfd90-9894-4d1f-807d-23e0a6acb548
Rassam, Patrice
2516d2de-abe9-4b88-b69a-7fa5bba29787
Khalid, Syma
90fbd954-7248-4f47-9525-4d6af9636394
Murray, Seán M.
8c6aefa5-dc51-4926-898c-859d733e8f50
Redfield, Christina
870a366a-9440-4f60-bf2a-ac8e8e864c29
Kleanthous, Colin
3d6d354c-bddf-4b64-8e4a-3f5b523802c2

Szczepaniak, Joanna, Holmes, Peter, Rajasekar, Karthik, Kaminska, Renata, Samsudin, Firdaus, Inns, Patrick George, Rassam, Patrice, Khalid, Syma, Murray, Seán M., Redfield, Christina and Kleanthous, Colin (2020) The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism. Nature Communications, 11 (1), [1305]. (doi:10.1038/s41467-020-15083-5).

Record type: Article

Abstract

Coordination of outer membrane constriction with septation is critical to faithful division in Gram-negative bacteria and vital to the barrier function of the membrane. This coordination requires the recruitment of the peptidoglycan-binding outer-membrane lipoprotein Pal at division sites by the Tol system. Here, we show that Pal accumulation at Escherichia coli division sites is a consequence of three key functions of the Tol system. First, Tol mobilises Pal molecules in dividing cells, which otherwise diffuse very slowly due to their binding of the cell wall. Second, Tol actively captures mobilised Pal molecules and deposits them at the division septum. Third, the active capture mechanism is analogous to that used by the inner membrane protein TonB to dislodge the plug domains of outer membrane TonB-dependent nutrient transporters. We conclude that outer membrane constriction is coordinated with cell division by active mobilisation-and-capture of Pal at division septa by the Tol system.

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More information

Accepted/In Press date: 13 February 2020
e-pub ahead of print date: 11 March 2020
Published date: 1 December 2020

Identifiers

Local EPrints ID: 439521
URI: http://eprints.soton.ac.uk/id/eprint/439521
ISSN: 2041-1723
PURE UUID: b4a91946-9fbf-4843-aebc-33fe2c819f8c
ORCID for Firdaus Samsudin: ORCID iD orcid.org/0000-0003-2766-4459
ORCID for Syma Khalid: ORCID iD orcid.org/0000-0002-3694-5044

Catalogue record

Date deposited: 24 Apr 2020 16:44
Last modified: 26 Nov 2021 03:05

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Contributors

Author: Joanna Szczepaniak
Author: Peter Holmes
Author: Karthik Rajasekar
Author: Renata Kaminska
Author: Firdaus Samsudin ORCID iD
Author: Patrick George Inns
Author: Patrice Rassam
Author: Syma Khalid ORCID iD
Author: Seán M. Murray
Author: Christina Redfield
Author: Colin Kleanthous

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