Yeast Heat Shock Transcription Factor N-terminal Activation Domains Are Unstructured As Probed by Heteronuclear NMR Spectroscopy

Overview

Journal Protein Sci

Specialty Biochemistry

Date 1996 Feb 1

PMID 8745404

Citations 12

Authors

H S Cho

C W Liu

F F Damberger

J G Pelton

H C NELSON

D E Wemmer

Affiliations

Soon will be listed here.

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.

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