Interaction of Fis protein with DNA: bending and specificity of binding.
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.
Bétermier
M
M
Laboratoire de Microbiologie et Génétique Moléculaire du CNRS, Toulouse, France.
Galas
D J
DJ
Chandler
M
M
D002352:Carrier Proteins / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D003850:Deoxyribonuclease I; D004586:Electrophoresis; D035021:Factor For Inversion Stimulation Protein; D034982:Integration Host Factors; D009690:Nucleic Acid Conformation; D010449:Peptide Mapping; D010957:Plasmids / Q000235:genetics; D011485:Protein Binding
D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D035021:Factor For Inversion Stimulation Protein; D034982:Integration Host Factors; D003850:Deoxyribonuclease I