Equilibria and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis

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ID: 290186
1981
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Abstract
We describe the use of gel electrophoresis in studies of equilibrium binding, site distribution, and kinetics of protein-DNA interactions. The method, which we call protein distribution analysis, is simple, sensitive and yields thermodynamically rigorous results. It is particularly well suited to studies of simultaneous binding of several proteins to a single nucleic acid. In studies of the lac repressor-operator interaction, we found that binding to the so-called third operator site (03) is 15–18 fold weaker than operator binding, and that the binding reactions with the first and third operators are uncoupled, implying that there is no communication between the sites. Pseudo-first order dissociation kinetics of the repressor-203 bp operator complex were found to be temperature sensitive, with ΔE of 80 kcal mol 1 above 29°C and 26 kcal mol −1 below. The half life of the complex (5 min at 21°C) is shorter than that reported for very high molecular weight operator-containing DNAs, but longer than values reported for much shorter fragments. The binding of lac repressor core to DNA could not be detected by this technique: the maximum binding constant consistent with this finding is 10 5 M −1 .
Reference Key
openalex_W2004563262 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Michael G. Fried, Donald M. Crothers
Journal Nucleic Acids Research
Year 1981
DOI
10.1093/nar/9.23.6505
URL
https://doi.org/10.1093/nar/9.23.6505
Keywords Keywords not found

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