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Yeast heat shock transcription factor N‐terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy
Author(s) -
Cho Ho S.,
Liu Corey W.,
Damberger Fred F.,
Pelton Jeffrey G.,
Nelson Hillary C. M.,
Wemmer David E.
Publication year - 1996
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560050210
Subject(s) - heteronuclear molecule , nuclear magnetic resonance spectroscopy , yeast , transcription factor , chemistry , heteronuclear single quantum coherence spectroscopy , heat shock protein , biophysics , biochemistry , biology , stereochemistry , gene
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 15 N[ 1 H] correlation and 15 N[ 1 H] 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.