Reference : DNA bending by the silencer protein NeP1 is modulated by TR and RXR.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
DNA bending by the silencer protein NeP1 is modulated by TR and RXR.
Arnold, R. [> > > >]
Burcin, M. [> > > >]
Kaiser, Bruno [Centre Hospitalier Universitaire de Liège - CHU > > Imagerie médicale >]
Muller, Marc mailto [Université de Liège - ULiège > Département des sciences de la vie > GIGA-R : Biologie et génétique moléculaire >]
Renkawitz, R. [> > > >]
Nucleic Acids Research
Oxford University Press
Yes (verified by ORBi)
United Kingdom
[en] Animals ; Binding Sites ; Cell Line, Transformed ; Cercopithecus aethiops ; Chickens ; DNA/chemistry/metabolism ; Hela Cells ; Humans ; Nucleic Acid Conformation ; Receptors, Retinoic Acid/metabolism ; Receptors, Thyroid Hormone/metabolism ; Repressor Proteins/metabolism ; Retinoid X Receptors ; Transcription Factors/metabolism
[en] NeP1 binds to the F1 silencer element of the chicken lysozyme gene and, in the presence of TR, v-ERBA or RAR, synergistically represses transcriptional activity. This repression involves a silencing mechanism acting independently of the relative promoter position. Here we show that NeP1 alone can induce a significant directed bend on DNA. The chicken homologue of human NeP1, CTCF, shows identical binding and bending properties. In contrast, the isolated DNA binding domain of CTCF efficiently binds DNA, but fails to confer bending. Similarly, the TR-RXR hetero- or homodimer, binding adjacent to NeP1 at the F2 sequence, do not show significant DNA bending. The binding of the T3 ligand to TR changes neither the magnitude nor the direction of the NeP1 induced bend. However, when all factors are bound simultaneously as a quaternary complex, the TR-RXR heterodimer changes the location of the bend center, the flexure angle and the bending direction.

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