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Default Yeast heat shock transcription factor N-terminal activation domains are unstructured

Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.

Related Articles Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.

Protein Sci. 1996 Feb;5(2):262-9

Authors: Cho HS, Liu CW, Damberger FF, Pelton JG, Nelson HC, Wemmer DE

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.

PMID: 8745404 [PubMed - indexed for MEDLINE]



Source: PubMed
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