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

Overview

Journal Mol Gen Genet

Specialties Genetics
Molecular Biology

Date 1984 Jan 1

PMID 6234449

Citations 2

Authors

D K Nag

D J Chattopadhyay

N C Mandal

Affiliations

Soon will be listed here.

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).

Citing Articles

Structure and function of the repressor of bacteriophage lambda. III. Molecular cloning of the high-affinity mutant cI gene of lambda and studies of the properties of the clones.

Das T, Mandal N Mol Gen Genet. 1986; 204(3):540-2.

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A single amino acid alteration in the initiation protein is responsible for the DNA overproduction phenotype of copy number mutants of plasmid R6K.

Inuzuka M, Wada Y EMBO J. 1985; 4(9):2301-7.

PMID: 3000771 PMC: 554501. DOI: 10.1002/j.1460-2075.1985.tb03930.x.

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