Functional consequences of the oligomeric assembly of proteorhodopsin.
Ontology highlight
ABSTRACT: The plasma membrane is the crucial interface between the cell and its exterior, packed with embedded proteins experiencing simultaneous protein-protein and protein-membrane interactions. A prominent example of cell membrane complexity is the assembly of transmembrane proteins into oligomeric structures, with potential functional consequences that are not well understood. From the study of proteorhodopsin (PR), a prototypical seven-transmembrane light-driven bacterial proton pump, we find evidence that the inter-protein interaction modulated by self-association yields functional changes observable from the protein interior. We also demonstrate that the oligomer is likely a physiologically relevant form of PR, as crosslinking of recombinantly expressed PR reveals an oligomeric population wit
SUBMITTER: Hussain S
PROVIDER: S-EPMC4374980 | biostudies-literature | 2015 Mar
REPOSITORIES: biostudies-literature
ACCESS DATA