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Genetics, Vol 120, 651-655, Copyright © 1988
INVESTIGATIONS |
Second-Site Revertants of Escherichia coli trp Repressor Mutants
L. S. Klig, D. L. Oxender and C. Yanofsky
Present address: Glaxo Institute for Molecular Biology, Rue des Acacias 46, 1211 Geneva 24, Switzerland.
Second-site reversion studies were performed with five missense mutants with defects in the trp repressor of Escherichia coli. These mutants were altered throughout the gene. The same unidirectional mutagen used in the isolation of these mutants, hydroxylamine, was used in reversion studies, to increase the liklihood that the revertants obtained would have second-site changes. Most of the second-site revertants were found to have the same amino acid substitutions detected previously as superrepressor changes. These second-site revertant repressors were more active in vivo than their parental mutant repressors, in the presence or absence of exogenous tryptophan. Apparently superrepressor changes at many locations in this protein can act globally to increase the activity of mutant repressors.
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