Article (Scientific journals)
DNA bending by the silencer protein NeP1 is modulated by TR and RXR.
Arnold, R.; Burcin, M.; Kaiser, Bruno et al.
1996In Nucleic Acids Research, 24 (14), p. 2640-7
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Keywords :
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
Abstract :
[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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Arnold, R.
Burcin, M.
Kaiser, Bruno ;  Centre Hospitalier Universitaire de Liège - CHU > Imagerie médicale
Muller, Marc  ;  Université de Liège - ULiège > Département des sciences de la vie > GIGA-R : Biologie et génétique moléculaire
Renkawitz, R.
Language :
English
Title :
DNA bending by the silencer protein NeP1 is modulated by TR and RXR.
Publication date :
1996
Journal title :
Nucleic Acids Research
ISSN :
0305-1048
eISSN :
1362-4962
Publisher :
Oxford University Press, Oxford, United Kingdom
Volume :
24
Issue :
14
Pages :
2640-7
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 24 September 2009

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