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

Autor:	Bryant JA; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom., Morris FC; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom., Knowles TJ; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.; School of Biosciences, University of Birmingham, Edgbaston, United Kingdom., Maderbocus R; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.; Institute for Cancer and Genomic Sciences, University of Birmingham, Edgbaston, United Kingdom., Heinz E; Infection & Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Clayton, Australia., Boelter G; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom., Alodaini D; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom., Colyer A; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom., Wotherspoon PJ; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom., Staunton KA; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom., Jeeves M; Institute for Cancer and Genomic Sciences, University of Birmingham, Edgbaston, United Kingdom., Browning DF; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom., Sevastsyanovich YR; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom., Wells TJ; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom., Rossiter AE; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom., Bavro VN; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom., Sridhar P; School of Biosciences, University of Birmingham, Edgbaston, United Kingdom., Ward DG; School of Biosciences, University of Birmingham, Edgbaston, United Kingdom., Chong ZS; Department of Chemistry, National University of Singapore, Singapore, Singapore., Goodall EC; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.; Institute for Molecular Bioscience, University of Queensland, St. Lucia, Australia., Icke C; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.; Institute for Molecular Bioscience, University of Queensland, St. Lucia, Australia., Teo AC; School of Life Sciences, The University of Warwick, Coventry, United Kingdom., Chng SS; Department of Chemistry, National University of Singapore, Singapore, Singapore.; School of Life Sciences, The University of Warwick, Coventry, United Kingdom., Roper DI; School of Life Sciences, The University of Warwick, Coventry, United Kingdom., Lithgow T; Infection & Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Clayton, Australia., Cunningham AF; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.; Institute of Inflammation and Immunotherapy, University of Birmingham, Edgbaston, United Kingdom., Banzhaf M; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom., Overduin M; School of Biosciences, University of Birmingham, Edgbaston, United Kingdom.; Department of Biochemistry, University of Alberta, Edmonton, Canada., Henderson IR; Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom.; Department of Chemistry, National University of Singapore, Singapore, Singapore.
Jazyk:	angličtina
Zdroj:	ELife [Elife] 2020 Dec 14; Vol. 9. Date of Electronic Publication: 2020 Dec 14.
DOI:	10.7554/eLife.62614
Abstrakt:	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. Competing Interests: JB, FM, TK, RM, EH, GB, DA, AC, PW, KS, MJ, DB, YS, TW, AR, VB, PS, DW, ZC, EG, CI, AT, SC, DR, TL, AC, MB, MO, IH No competing interests declared (© 2020, Bryant et al.)
Databáze:	MEDLINE
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