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Lipid interactions with bacterial channels: fluorescence studies

Lipid interactions with bacterial channels: fluorescence studies
Lipid interactions with bacterial channels: fluorescence studies
Interactions between a membrane protein and the lipid molecules that surround it in the membrane are important in determining the structure and function of the protein. These interactions can be pictured at the molecular level using fluorescence spectroscopy, making use of the ability to introduce tryptophan residues into regions of interest in bacterial membrane proteins. Fluorescence quenching methods have been developed to study lipid binding separately on the two sides of the membrane. Lipid binding to the surface of the mechanosensitive channel MscL is heterogeneous, with a hot-spot for binding anionic lipid on the cytoplasmic side, associated with a cluster of three positively charged residues. The environmental sensitivity of tryptophan fluorescence emission has been used to identify the residues at the ends of the hydrophobic core of the second transmembrane ?-helix in MscL. The efficiency of hydrophobic matching between MscL and the surrounding lipid bilayer is high. Fluorescence quenching methods can also be used to study binding of lipids to non-annular sites such as those between monomers in the homotetrameric potassium channel KcsA.
bacterial channel, fluorescence, KcsA, lipid-protein interaction, mechanosensitive channel, potassium channel
0300-5127
905-909
Powl, A.M.
58e5cab2-1c71-412b-97ca-39604b73b08c
Carney, J.
840c4dbe-b1a8-4cde-9281-dd8880e58078
Marius, P.
2022328d-4410-4ac3-902d-5e1c87b3c958
East, J.M.
9fe7f794-1d89-4935-9a99-b831d786056e
Lee, A.G.
0891914c-e0e2-4ee1-b43e-1b70eb072d8e
Powl, A.M.
58e5cab2-1c71-412b-97ca-39604b73b08c
Carney, J.
840c4dbe-b1a8-4cde-9281-dd8880e58078
Marius, P.
2022328d-4410-4ac3-902d-5e1c87b3c958
East, J.M.
9fe7f794-1d89-4935-9a99-b831d786056e
Lee, A.G.
0891914c-e0e2-4ee1-b43e-1b70eb072d8e

Powl, A.M., Carney, J., Marius, P., East, J.M. and Lee, A.G. (2005) Lipid interactions with bacterial channels: fluorescence studies. Biochemical Society Transactions, 33 (5), 905-909. (doi:10.1042/BST20050905).

Record type: Article

Abstract

Interactions between a membrane protein and the lipid molecules that surround it in the membrane are important in determining the structure and function of the protein. These interactions can be pictured at the molecular level using fluorescence spectroscopy, making use of the ability to introduce tryptophan residues into regions of interest in bacterial membrane proteins. Fluorescence quenching methods have been developed to study lipid binding separately on the two sides of the membrane. Lipid binding to the surface of the mechanosensitive channel MscL is heterogeneous, with a hot-spot for binding anionic lipid on the cytoplasmic side, associated with a cluster of three positively charged residues. The environmental sensitivity of tryptophan fluorescence emission has been used to identify the residues at the ends of the hydrophobic core of the second transmembrane ?-helix in MscL. The efficiency of hydrophobic matching between MscL and the surrounding lipid bilayer is high. Fluorescence quenching methods can also be used to study binding of lipids to non-annular sites such as those between monomers in the homotetrameric potassium channel KcsA.

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More information

Published date: 1 November 2005
Keywords: bacterial channel, fluorescence, KcsA, lipid-protein interaction, mechanosensitive channel, potassium channel

Identifiers

Local EPrints ID: 56596
URI: https://eprints.soton.ac.uk/id/eprint/56596
ISSN: 0300-5127
PURE UUID: 0724730d-a138-45ea-9ca8-06ffeef7734e

Catalogue record

Date deposited: 07 Aug 2008
Last modified: 17 Jul 2017 14:30

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