The orientation of halorhodopsin in the cell membrane of halobacteria.
The orientation of the light-driven chloride pump, halorhodopsin, in the membrane was determined using antibodies directed against a synthetic peptide which represents the C-terminal segment of the protein. Antibodies against this decapeptide did not bind to right-side-out cell vesicles. Partial inversion by sonication or lysis under low salt conditions exposed this COOH-terminal antigenic site. Antibody binding was removed by preincubation with the decapeptide. The COOH terminus of the molecule is therefore located on the cytoplasmic surface of the membrane.
May
K M
KM
Max-Planck-Institut für Biochemie, Martinsried, Federal Republic of Germany.
Jay
F A
FA
Oesterhelt
D
D
D000595:Amino Acid Sequence; D001436:Bacteriorhodopsins / Q000032:analysis*; D002462:Cell Membrane / Q000032:analysis*; D003593:Cytoplasm / Q000032:analysis; D004797:Enzyme-Linked Immunosorbent Assay; D006217:Halobacterium / Q000032:analysis* / Q000648:ultrastructure; D025602:Halorhodopsins; D008969:Molecular Sequence Data; D011487:Protein Conformation
D025602:Halorhodopsins; D001436:Bacteriorhodopsins