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Position of the lacZX90 mutation and hybridization between complete and incomplete beta-galactosidase
Author(s) -
Wlodzimierz Mandecki,
Audrée V. Fowler,
Irving Zabin
Publication year - 1981
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.147.2.694-697.1981
Subject(s) - biology , tyrosine , mutation , nonsense mutation , enzyme , beta galactosidase , biochemistry , stop codon , methionine , microbiology and biotechnology , amino acid , gene , escherichia coli , missense mutation
The position of the termination codon in lacZX90 was determined by isolation of a lac+ revertant. Lysine was found to replace tyrosine at position 1,012 of beta-galactosidase, indicating that X90 protein lacked the carboxyl-terminal 10 residues. A heat- and urea-sensitive hybrid enzyme was formed in vivo when supC, which supplies tyrosine to the position in the polypeptide corresponding to the nonsense codon, was used to suppress lacZX90. This result shows that suppression that adds back the original amino acid may not lead to the production of the wild-type enzyme if the latter is multimeric, because incomplete chains can be incorporated into the oligomer.

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