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.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, Non-P.H.S.
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Base Sequence
-
Binding Sites
-
Circular Dichroism
-
DNA, Fungal / metabolism
-
Fungal Proteins / chemistry*
-
Fungal Proteins / metabolism
-
Heat-Shock Proteins / chemistry*
-
Heat-Shock Proteins / metabolism
-
Kluyveromyces / chemistry*
-
Kluyveromyces / metabolism
-
Magnetic Resonance Spectroscopy*
-
Molecular Sequence Data
-
Recombinant Proteins / chemistry
-
Saccharomyces cerevisiae / chemistry*
-
Saccharomyces cerevisiae / metabolism
-
Transcription, Genetic
Substances
-
DNA, Fungal
-
Fungal Proteins
-
Heat-Shock Proteins
-
Recombinant Proteins