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A perfectly symmetric lac operator binds the lac repressor very tightly

J R Sadler, H Sasmor, and J L Betz
PNAS November 1, 1983 80 (22) 6785-6789; https://doi.org/10.1073/pnas.80.22.6785
J R Sadler
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H Sasmor
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J L Betz
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Abstract

A completely symmetric DNA segment has been constructed that binds the lactose repressor of Escherichia coli 10-fold more tightly than does the natural lactose operator sequence. This tight-binding operator is an inverted repeat of a 15-base-pair segment from the left half of the natural operator sequence, the inversion being about the point indicated by the arrow shown below: (sequence in text) where the upper sequence is the natural operator and the lower sequence is the symmetric operator. The increased affinity of repressor for this symmetric sequence supports the idea that the tetrameric repressor is designed for a two-module binding to DNA, presumably via two (or two pairs) of its identical subunits. The natural operator is apparently "flawed" by "incorrect" base pairs in the right operator half and by an "incorrect" spacing between the operator halves with respect to maximal repressor binding.

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A perfectly symmetric lac operator binds the lac repressor very tightly
J R Sadler, H Sasmor, J L Betz
Proceedings of the National Academy of Sciences Nov 1983, 80 (22) 6785-6789; DOI: 10.1073/pnas.80.22.6785

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A perfectly symmetric lac operator binds the lac repressor very tightly
J R Sadler, H Sasmor, J L Betz
Proceedings of the National Academy of Sciences Nov 1983, 80 (22) 6785-6789; DOI: 10.1073/pnas.80.22.6785
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  • Effector Overlap between the lac and mel Operons of Escherichia coli: Induction of the mel Operon with {beta}-Galactosides
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  • Develop reusable and combinable designs for transcriptional logic gates
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  • The Type III Pantothenate Kinase Encoded by coaX Is Essential for Growth of Bacillus anthracis
  • A Single, Specific Thymine Mutation in the ComK-Binding Site Severely Decreases Binding and Transcription Activation by the Competence Transcription Factor ComK of Bacillus subtilis
  • Adaptation of a Luciferase Gene Reporter and lac Expression System to Borrelia burgdorferi
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  • Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator O1 through alternative conformations of its DNA-binding domain
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Proceedings of the National Academy of Sciences: 115 (38)
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