Architectural transcription factors: proteins that remodel DNA
Article Abstract:
A particular set of accessory proteins called architectural transcription factors has been found to be bound to either the major or the minor groove faces of DNA molecules which result to the alteration of the trajectory of the double helix, thus, remodeling the DNA. Prokaryotic architectural transcription factors include, among others, the cAMP receptor protein and integration host factor. In eukaryotes, three architectural transcription factors have been identified, the TATA box-binding protein, SRY and LEF-1. The kinetics and thermodynamic properties of nucleoprotein complexes arising from the binding of these factors to DNA are yet to be investigated.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
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Molecular basis of human 46X, Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex
Article Abstract:
Nuclear magnetic resonance of the high mobility group domain of SRY (hSRY-HMG) protein, the activator of the Mullerian inhibiting substance gene, revealed a twisted L-shape with a concave surface. Binding of the DNA to the minor groove of this surface induces conformational changes in the DNA complex. The helix unwinds from its normal 70-80 degree bend to form a classical A- and B-DNA. An examination of the new configuration revealed a large family of eukaryotic proteins, HMG-1/HMG-2, which induces point mutations causing 46X, Y sex reversal.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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The solution structure of the human ETS1-DNA complex reveals a novel mode of binding and true side chain intercalation
Article Abstract:
The structure of the complex of the human ETS1 (hETS1) oncogene's DNA binding domain with DNA shows structural differences from other such helix-turn-helix (HTH) protein complexes. Major groove recognition is by the C-terminal of the HTH. Minor groove recognition is by true intercalation of the hETS1 side chain. The intercalation twists and widens the minor groove. There is significant rotation in the position of the HTH in the complex with respect to major grooves. Stimulation of transcription by hETS1 is probably due to the twist.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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