title: Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.
abstract: The structure and dynamics of the N-terminal activation domains of the yeast heat shock transcription factors of Kluyveromyces lactis and Saccharomyces cerevisiae were probed by heteronuclear 15N[1H] correlation and 15N[1H] NOE NMR studies. Using the DNA-binding domain as a structural reference, we show that the protein backbone of the N-terminal activation domain undergoes rapid, large-amplitude motions and is therefore unstructured. Difference CD data also show that the N-terminal activation domain remains random-coil, even in the presence of DNA. Implications for a "polypeptide lasso" model of transcriptional activation are discussed.
authors: Department of Chemistry, University of California, Berkeley 94720, USA.
authors: H S
authors: HS
authors: Cho
authors: C W
authors: CW
authors: Liu
authors: F F
authors: FF
authors: Damberger
authors: J G
authors: JG
authors: Pelton
authors: H C
authors: HC
authors: Nelson
authors: D E
authors: DE
authors: Wemmer
mesh_terms: D001483:Base Sequence; D001665:Binding Sites; D002942:Circular Dichroism; D004271:DNA, Fungal / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism; D007716:Kluyveromyces / Q000737:chemistry* / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000378:metabolism; D014158:Transcription, Genetic
chemical_list: D004271:DNA, Fungal; D005656:Fungal Proteins; D006360:Heat-Shock Proteins; D011994:Recombinant Proteins