Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.
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.
Cho
H S
HS
Department of Chemistry, University of California, Berkeley 94720, USA.
Liu
C W
CW
Damberger
F F
FF
Pelton
J G
JG
Nelson
H C
HC
Wemmer
D E
DE
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
D004271:DNA, Fungal; D005656:Fungal Proteins; D006360:Heat-Shock Proteins; D011994:Recombinant Proteins