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Structure and function of the repressor of bacteriophage lambda

II. Isolation and characterization of a lambda mutant which produces repressor having higher affinity for operators

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Summary

By mutagenizing a λcItscI857) lysogen, a λ mutant has been isolated with a wild-type phenotype. This mutant phage lysogenizes with low efficiency and produces a low burst. Though the initial rates of repressor synthesis in Escherichia coli after infection with wild-type and mutant λ are the same, the maximum level of repressor that is synthesized in the latter case is only about 30% of that synthesized in the former. Virulent λ plates on the lysogen of mutant λ with slightly less efficiency producing very tiny plaques. Operator-binding studies made in vitro with purified mutant and wild-type repressors show that the binding curve of the former repressor is a rectangular hyperbola while that of the latter is sigmoid. The half-lives of the complexes of mutant and wild-type repressors with right operator are 133 and 27 min, respectively. All these results suggest that the mutant repressor possibly has a higher affinity for the operators. This mutant has been named λcIha (ha=high affinity).

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Communicated by W. Arber

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Nag, D.K., Chattopadhyay, D.J. & Mandal, N.C. Structure and function of the repressor of bacteriophage lambda. Molec. Gen. Genet. 194, 373–376 (1984). https://doi.org/10.1007/BF00425547

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  • DOI: https://doi.org/10.1007/BF00425547

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