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Membrane protein-lipid selectivity: enhancing sensitivity for modeling FRET data.

Carme Suárez-Germà¹, Luís M S Loura, Manuel Prieto

¹Institut de Nanociència i Nanotecnologia IN²UB, Parc Científic de Barcelona, 08028 Barcelona, Spain.

The Journal of Physical Chemistry. B

|February 3, 2012

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Förster resonance energy transfer (FRET) reveals membrane protein lipid selectivity. This study quantified distances between tryptophan lactose permease (LacY) and pyrene-labeled lipids, finding LacY prefers phosphatidylethanolamine (PE) over phosphatidylglycerol (PG) and phosphatidylcholine (PC).

Area of Science:

Biophysics
Membrane Protein Biochemistry
Spectroscopy

Background:

Förster resonance energy transfer (FRET) is crucial for characterizing membrane protein lipid selectivity.
Studying protein-lipid interactions requires analyzing multiple donor-acceptor pairs and distances, especially with annular lipids.
Theoretical analysis using binomial distribution is necessary for FRET experiments involving multiple acceptors around membrane proteins.

Purpose of the Study:

To quantify the lipid selectivity of lactose permease (LacY) from Escherichia coli using FRET.
To determine the probability of annular site occupation and relative association constants for different phospholipids.
To investigate the role of acyl chains in phospholipid-protein interactions.

Main Methods:

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Performed FRET measurements between single tryptophan LacY (W151/C154G) and pyrene-labeled phospholipids (PE, PG, PC).

Reconstituted LacY in pure phospholipids doped with 1.5% labeled phospholipids at 25 and 37 °C.

Applied a theoretical model based on binomial distribution to experimental FRET efficiencies and analyzed pyrene monomer/excimer emission spectra.

Main Results:

Calculated the probability of annular site occupation and relative association constants between LacY and labeled phospholipids.
Observed higher selectivity of LacY for phosphatidylethanolamine (PE) compared to phosphatidylglycerol (PG) and phosphatidylcholine (PC).
Demonstrated a significant role of acyl chains in the overall phospholipid-protein interactions.

Conclusions:

FRET analysis, combined with a theoretical model, effectively characterizes membrane protein lipid selectivity.
LacY exhibits a preference for PE lipids, suggesting specific acyl chain interactions influence its binding.
The study provides insights into the structural basis of LacY's lipid preference and its functional implications.