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Dynamics of crowded vesicle: local and global responses to membrane composition

Dynamics of crowded vesicle: local and global responses to membrane composition
Dynamics of crowded vesicle: local and global responses to membrane composition
The bacterial cell envelope is composed of a mixture of different lipids and proteins, making it an inherently complex organelle. The interactions between integral membrane proteins and lipids are crucial for their respective spatial localization within bacterial cells. We have employed microsecond timescale coarse-grained molecular dynamics simulations of vesicles of varying sizes and with a range of protein and lipid compositions, and used novel approaches to measure both local and global system dynamics, the latter based on spherical harmonics analysis. Our results suggest that both hydrophobic mismatch, enhanced by embedded membrane proteins, and curvature based sorting, due to different modes of undulation, may drive assembly in vesicular systems. Interestingly, the modes of undulation of the vesicles were found to be altered by the specific protein and lipid composition of the vesicle. Strikingly, lipid dynamics were shown to be coupled to proteins up to 6 nm from their surface, a substantially larger distance than has previously been observed, resulting in multi-layered annular rings enriched with particular types of phospholipid. Such large protein-lipid complexes may provide a mechanism for long-range communication. Given the complexity of bacterial membranes, our results suggest that subtle changes in lipid composition may have major implications for lipid and protein sorting under a curvature-based membrane-sorting model.
1932-6203
1-18
Holdbrook, Daniel
05d5d888-d89c-4d3c-8e95-a16a90d67876
Huber, Roland G.
114d3558-3288-4a57-87cf-c712953a803a
Piggot, Thomas
75829b71-d73b-43d1-b24f-3e70c2c4d0c8
Bond, Peter J.
08f46940-85e8-44c4-a368-d94342a10fd6
Khalid, Syma
90fbd954-7248-4f47-9525-4d6af9636394
Holdbrook, Daniel
05d5d888-d89c-4d3c-8e95-a16a90d67876
Huber, Roland G.
114d3558-3288-4a57-87cf-c712953a803a
Piggot, Thomas
75829b71-d73b-43d1-b24f-3e70c2c4d0c8
Bond, Peter J.
08f46940-85e8-44c4-a368-d94342a10fd6
Khalid, Syma
90fbd954-7248-4f47-9525-4d6af9636394

Holdbrook, Daniel, Huber, Roland G., Piggot, Thomas, Bond, Peter J. and Khalid, Syma (2016) Dynamics of crowded vesicle: local and global responses to membrane composition. PLoS ONE, 11 (6), 1-18. (doi:10.1371/journal.pone.0156963).

Record type: Article

Abstract

The bacterial cell envelope is composed of a mixture of different lipids and proteins, making it an inherently complex organelle. The interactions between integral membrane proteins and lipids are crucial for their respective spatial localization within bacterial cells. We have employed microsecond timescale coarse-grained molecular dynamics simulations of vesicles of varying sizes and with a range of protein and lipid compositions, and used novel approaches to measure both local and global system dynamics, the latter based on spherical harmonics analysis. Our results suggest that both hydrophobic mismatch, enhanced by embedded membrane proteins, and curvature based sorting, due to different modes of undulation, may drive assembly in vesicular systems. Interestingly, the modes of undulation of the vesicles were found to be altered by the specific protein and lipid composition of the vesicle. Strikingly, lipid dynamics were shown to be coupled to proteins up to 6 nm from their surface, a substantially larger distance than has previously been observed, resulting in multi-layered annular rings enriched with particular types of phospholipid. Such large protein-lipid complexes may provide a mechanism for long-range communication. Given the complexity of bacterial membranes, our results suggest that subtle changes in lipid composition may have major implications for lipid and protein sorting under a curvature-based membrane-sorting model.

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More information

Accepted/In Press date: 22 May 2016
e-pub ahead of print date: 16 June 2016
Organisations: Computational Systems Chemistry

Identifiers

Local EPrints ID: 402196
URI: http://eprints.soton.ac.uk/id/eprint/402196
ISSN: 1932-6203
PURE UUID: 45fe7967-dc16-4d2c-8634-27e6639ff70c
ORCID for Syma Khalid: ORCID iD orcid.org/0000-0002-3694-5044

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Date deposited: 03 Nov 2016 14:26
Last modified: 07 Oct 2020 01:54

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Contributors

Author: Daniel Holdbrook
Author: Roland G. Huber
Author: Thomas Piggot
Author: Peter J. Bond
Author: Syma Khalid ORCID iD

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