Paramagnetic Relaxation Enhancement Reveals Oligomerization Interface of a Membrane Protein

Protein–protein interactions play critical roles in cellular function and oligomerization of membrane proteins is a commonly observed phenomenon. Determining the oligomerization state and defining the intermolecular interface in the bilayer is generally a difficult task. Here, we use site-specific s...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2012-10, Vol.134 (41), p.16995-16998
Main Authors: Wang, Shenlin, Munro, Rachel A, Kim, So Young, Jung, Kwang-Hwan, Brown, Leonid S, Ladizhansky, Vladimir
Format: Article
Language:English
Subjects:
Anabaena - chemistry
Sensory Rhodopsins - chemistry
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Summary:Protein–protein interactions play critical roles in cellular function and oligomerization of membrane proteins is a commonly observed phenomenon. Determining the oligomerization state and defining the intermolecular interface in the bilayer is generally a difficult task. Here, we use site-specific spin labeling to demonstrate that relaxation enhancements induced by covalently attached paramagnetic tag can provide distance restraints defining the intermonomer interface in oligomers formed by a seven-helical transmembrane protein Anabaena Sensory Rhodopsin (ASR). We combine these measurements with visible CD spectroscopy and cross-linking experiments to demonstrate that ASR forms tight trimers in both detergents and lipids.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja308310z