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Reference: Saudek V, et al. (1991) Solution structure of the basic region from the transcriptional activator GCN4. Biochemistry 30(5):1310-7

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Abstract


The structure of the basic region (i.e., the region responsible for sequence-specific binding to DNA) of the transcriptional activator GCN4 was studied. Two peptide fragments containing either the basic region alone (residues 240-280) or the basic and the dimerization leucine zipper domains (220-280) were synthesized and investigated by nuclear magnetic resonance and circular dichroic spectroscopy. The basic region in the absence of DNA appears as a mobile flexible segment folded into a loose helix. The helical stability increases upon addition of trifluoroethanol and/or lowering of the temperature. Dimerization via the leucine zipper does not affect the three-dimensional structure of the basic region. Possible consequences for the binding to DNA are discussed.

Reference Type
Journal Article
Authors
Saudek V, Pasley HS, Gibson T, Gausepohl H, Frank R, Pastore A
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