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PMID: 8745404 Published · ppublish English Journal Article 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.

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

Protein science : a publication of the Protein Society ·Vol. 5 ·No. 2 ·1996-02-00 ·Pages 262-9

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

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.

MeSH Terms
Base Sequence Binding Sites Circular Dichroism DNA, Fungal/metabolism Fungal Proteins/chemistry,metabolism Heat-Shock Proteins/chemistry,metabolism Kluyveromyces/chemistry,metabolism Magnetic Resonance Spectroscopy Molecular Sequence Data Recombinant Proteins/chemistry Saccharomyces cerevisiae/chemistry,metabolism Transcription, Genetic
Chemicals
DNA, Fungal Fungal Proteins Heat-Shock Proteins Recombinant Proteins
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Cho H S
Department of Chemistry, University of California, Berkeley 94720, USA.
Liu C W
Damberger F F
Pelton J G
Nelson H C
Wemmer D E
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Article Info
Journal
Protein science : a publication of the Protein Society
Abbr.
Protein Sci
ISSN
0961-8368
Published
1996-02-00
Pages
262-9
Language
English
Region
United States
NLM ID
9211750
PMCID
PMC2143352
Subset
IM
Grants
NIGMS NIH HHS · GM08295 · United States
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