Solution structure of the POU-specific DNA-binding domain of Oct-1
Article Abstract:
Nuclear magnetic resonance was used to determine the solution structure of the POU-specific DNA-binding domain of transcription factor Oct-1. Four alpha-helices are connected by short loops with helices I and IV in a parallel coiled-coil arrangement. There is an apparent similarity between the folding topology and that of the bacteriophage lambda-repressor and 434 repressor. Helix III appears to be the mediator in DNA-binding. A model for the POU-DNA complex is presented.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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The sound of silence
Article Abstract:
A study of the role of ligand-dependent transcription factors in the absence of their ligands shows that these transcription factors silence basal transcription in these circumstances. They also behave as heterodimers and potent repressors with the reversed polarities. Silencing is achieved by these receptors to increase target-gene specificity of certain elements. The potential of these results in studying the physiological role of trans-repression is discussed.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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Structural basis for DNA bending by the architectural transcription factor LEF-1
Article Abstract:
Minor groove binding and protein-induced DNA bending can be explored through the nuclear magnetic resonance exploration of the interaction between the lymphoid enhancer-binding factor (LEF-1) and a high-mobility-group (HMG) domain. The interaction structure shows the mechanism of the involvement of LEF-1 in the regulation of thymocyte differentiation and organogenesis.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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