The lac repressor and its N-terminal headpiece can bind a mini-operator containing a hairpin loop made of a hexaethylene glycol chain

• Published in: FEBS letters Vol. 288; no. 1-2; pp. 101 - 104
• Main Authors: Maurizot, J.C., Chevrie, K., Durand, M., Thuong, N.T.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 19-08-1991; Elsevier
• Subjects: Base Sequence; Biological and medical sciences; Circular Dichroism; DNA-Binding Proteins - metabolism; DNA—protein interaction; Escherichia coli; Escherichia coli - genetics; Ethylene Glycol; Ethylene Glycols - metabolism; Fundamental and applied biological sciences. Psychology; Hairpin; Headpiece; Interactions. Associations; Intermolecular phenomena; Lac Operon - physiology; Lac repressor; Modified oligonucleotide; Molecular biophysics; Molecular Sequence Data; Nucleic Acid Conformation; Oligonucleotides - metabolism; Operator Regions, Genetic - physiology; Peptide Fragments - metabolism; Repressor Proteins - metabolism; Spectrophotometry, Ultraviolet; Hairpin; DNA—protein interaction; Headpiece; Lac repressor; Modified oligonucleotide; Chemical modification; Hairpin loop; Transcription operator; Stabilization; Circular dichroism spectrometry; Molecular interaction; Transcription repressor; Oligodeoxyribonucleotide; N terminal peptide
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(91)81012-W

The binding of the lac repressor and the lac repressor N-terminal headpiece to a mini-operator with a hairpin loop made of a hexaethylene glycol chain was investigated using circular dichroism spectroscopy. The Iac repressor's headpiece binds to the modified mini-operator with the same affinity as to a mini-operator of the same sequence without the hexaethylene glycol loop. The conformational effect due to the binding is not affected by the presence of the hexaethylene loop. It is also shown that the entire lac repressor binds to this modified mini-operator inducing a conformational change.