Abstract
Purple membrane (PM) from Halobacterium salinarum has been studied by many groups and is commonly described as a flat 2-D crystalline membrane microdomain which contains a hexagonal crystalline lattice of bacteriorhodopsin (BR) trimers in a stoichiometric ratio of 10:1 between lipids and BR. BR is the key protein in the halobacterial photosynthetic system and acts as a light-driven proton pump. Upon absorption of a photon, BR undergoes a cyclic series of intramolecular changes, among them a transient "wedge-like" geometrical change of the protein due to a tilt in helix F, one of the seven alpha-helical domains of BR. Due to the strong coupling between the BRs in the crystalline lattice, this may affect membrane topography. In nature, only low light levels occur and the total number of BRs in the "wedge-shaped" state is negligible. For mutated PMs like PM-D85T and PM-D85N (PM-D85X, X = neutral residue), the change of the membrane topography can be triggered in a pH-dependent manner. PMs containing BR-D85X look like "cups" at certain pH values. How does nature deal with a mutated PM like PM-D96G/F171C/F219L (PM-Tri) which comprises permanently "wedge-shaped" BRs and how does this influence membrane assembly? Astonishingly, we observed that PM-Tri is flat. Obviously, the morphology of Halobacterium salinarum is highly conserved and requires flat PMs to be assembled. We found that the lipid content of PM-Tri is specifically altered to assemble a hexagonal crystalline PM-Tri lattice of flat topography.
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