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- W2017254890 abstract "The Escherichia coli Fis protein is a dimeric DNA-binding protein whose specific binding sites share a weak consensus sequence. Use of the gel retardation technique indicates that binding of Fis on a linear DNA fragment leads to the formation of a ladder of defined retarded complexes, independently of the presence of a specific site. This non-specific binding of Fis is consistent with a model where equivalent low-affinity sites on a given fragment would be bound randomly and independently of each other by consecutive Fis dimers. Evidence is presented that non-specific binding of Fis can, however, induce an apparent site-specific conformational change in the DNA. This observation is discussed in terms of a model in which each Fis:DNA complex detected in gel retardation experiments actually represents a dynamic equilibrium of a fixed number of Fis dimers distributed on the fragment." @default.
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- W2017254890 date "1994-01-01" @default.
- W2017254890 modified "2023-10-16" @default.
- W2017254890 title "Interaction of Fis protein with DNA: Bending and specificity of binding" @default.
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- W2017254890 doi "https://doi.org/10.1016/0300-9084(94)90021-3" @default.
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