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Repressor--operator interaction in the lac operon. II. Observations at the tyrosines and tryptophans



Repressor--operator interaction in the lac operon. II. Observations at the tyrosines and tryptophans



Journal of Molecular Biology 161(3): 417-438



19F-NMR spectroscopy was used to examine the interactions of 3-fluorotyrosine and 5-fluorotryptophan-substituted wild-type lactose operon repressors from Escherichia coli and lac operator DNA. A survey of inducer and salt concentration effects on the repressor-operator complex is presented. A scheme for the interactions between the repressor, operator and inducer, in both binary and ternary complexes is proposed. The scheme accommodates previous results. The complex between the tetrameric repressor and one 36 base pair operator DNA fragment results in the simultaneous broadening of the resonances from all 4 N-terminal DNA binding domains. The actual contacts made by these binding domains are similar but probably not identical. The binding of the inducer molecule to the tetrameric repressor results in an allosteric change that can be monitored by the increased intensity of the resonances from individual tyrosine residues in the N-terminal binding domain. This increased N-terminal tyrosine resonance intensity in the complex is transmitted to repressor subunits that have not yet bound an inducer molecule.

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Accession: 006315078

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PMID: 6759662


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