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Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation

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Bryant, Jack Alfred, Morris, Faye C., Knowles, Timothy J., Maderbocus, Riyaz, Heinz, Eva, Boelter, Gabriela, Alodaini, Dema, Colyer, Adam, Wotherspoon, Peter J., Staunton, Kara A. et al.
(2020) Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation. eLife, 9 . e62614. doi:10.7554/eLife.62614

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Official URL: http://dx.doi.org/10.7554/eLife.62614

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Abstract

The Gram-negative outer-membrane envelops the bacterium and functions as a permeability barrier against antibiotics, detergents, and environmental stresses. Some virulence factors serve to maintain the integrity of the outer membrane, including DolP (formerly YraP) a protein of unresolved structure and function. Here, we reveal DolP is a lipoprotein functionally conserved amongst Gram-negative bacteria and that loss of DolP increases membrane fluidity. We present the NMR solution structure for Escherichia coli DolP, which is composed of two BON domains that form an interconnected opposing pair. The C-terminal BON domain binds anionic phospholipids through an extensive membrane:protein interface. This interaction is essential for DolP function and is required for sub-cellular localisation of the protein to the cell division site, providing evidence of subcellular localisation of these phospholipids within the outer membrane. The structure of DolP provides a new target for developing therapies that disrupt the integrity of the bacterial cell envelope.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Q Science > QP Physiology
Q Science > QR Microbiology
Divisions: Faculty of Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Gram-negative bacteria , Phospholipids, Protein binding, Hydrophobic surfaces
Journal or Publication Title: eLife
Publisher: eLife Sciences Publications Ltd.
ISSN: 2050-084X
Official Date: 14 December 2020
Dates:
DateEvent
14 December 2020Published
11 December 2020Accepted
Date of first compliant deposit: 18 January 2021
Volume: 9
Article Number: e62614
DOI: 10.7554/eLife.62614
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
BB/M00810X/1 [BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/L00335X/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/ P009840/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
RGPIN-2018–04994[NSERC] Natural Sciences and Engineering Research Council of Canadahttp://dx.doi.org/10.13039/501100000038
RCP-12–002CCampus Alberta Neurosciencehttp://dx.doi.org/10.13039/100013054

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