Bacteriorhodopsin mutants of Halobacterium sp. GRB. II. Characterization of mutants.
The bacterioopsin genes of Halobacterium sp. GRB (Ebert, K., Goebel, W., and Pfeifer, F. (1984) Mol. & Gen. Genet. 194, 91-97) wild type and 10 independent mutants of different phenotypes have been cloned and sequenced. The wild type gene has two conservative changes compared to the gene of Halobacterium halobium, so that the proteins of the two species are identical. Six different mutations at five different codons have been found, leading to the following amino acid changes compared to the wild type: Trp10----Cys (three cases), Tyr57----Asn, Asp85----Glu, Asp06----Asn (three cases), Asp96----Gly, Trp138----Arg. A first characterization of the mutant proteins is given, and their implications for models of bacteriorhodopsin structure and function are discussed.
Soppa
J
J
Max-Planck-Institut für Biochemie, Martinsried, West Germany.
Otomo
J
J
Straub
J
J
Tittor
J
J
Meessen
S
S
Oesterhelt
D
D
D000595:Amino Acid Sequence; D001216:Asparagine / Q000235:genetics; D001224:Aspartic Acid / Q000235:genetics; D001436:Bacteriorhodopsins / Q000235:genetics* / Q000302:isolation & purification; D001483:Base Sequence; D003001:Cloning, Molecular; D003545:Cysteine / Q000235:genetics; D005798:Genes, Bacterial; D005971:Glutamates / Q000235:genetics; D018698:Glutamic Acid; D005998:Glycine / Q000235:genetics; D006217:Halobacterium / Q000145:classification / Q000235:genetics*; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D014364:Tryptophan / Q000235:genetics; D014443:Tyrosine / Q000235:genetics
D005971:Glutamates; D001224:Aspartic Acid; D018698:Glutamic Acid; D014443:Tyrosine; D001436:Bacteriorhodopsins; D001216:Asparagine; D014364:Tryptophan; D003545:Cysteine; D005998:Glycine