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  • Title: 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.
    Author: Nag DK, Chattopadhyay DJ, Mandal NC.
    Journal: Mol Gen Genet; 1984; 194(3):373-6. PubMed ID: 6234449.
    Abstract:
    By mutagenizing a lambda cIts (lambda cI857) lysogen, a lambda 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 lambda 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 lambda plates on the lysogen of mutant lambda 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 lambda cIha (ha = high affinity).
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