Anion selectivity and pumping mechanism of halorhodopsin.
Comparison of the amino acid sequences in the A-B and B-C interhelical loop segments in all bacteriorhodopsins and halorhodopsins has shed light on the anion selectivity and pumping mechanism of halorhodopsin. The nucleotide sequences of two haloopsins from two new halobacterial strains, shark and port, have been determined, and shark halorhodopsin was functionally overexpressed in Halobacterium halobium. Although a series of six amino acid residues (EMPAGH) in the B-C interhelical loop segment was substituted by QMPPGH, all putative charged residues were conserved. It was also shown that His-95 mutants had lower pumping activity in low chloride concentrations. These results further support the hypothesis that His-95 is important in the halorhodopsin function.
Otomo
J
J
PRESTO, JRDC and Advanced Research Laboratory, Hitachi, Ltd., Saitama, Japan.
D000595:Amino Acid Sequence; D001436:Bacteriorhodopsins / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism*; D002712:Chlorides / Q000378:metabolism*; D017124:Conserved Sequence; D019617:Halobacterium salinarum / Q000145:classification / Q000378:metabolism*; D025602:Halorhodopsins; D006639:Histidine; D016623:Ion Pumps / Q000378:metabolism; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D002712:Chlorides; D025602:Halorhodopsins; D016623:Ion Pumps; D011994:Recombinant Proteins; D006639:Histidine; D001436:Bacteriorhodopsins