Related ArticlesYeast 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.
Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR.
Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR.
Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR.
Proc Natl Acad Sci U S A. 2011 May 31;108(22):E169-76
Authors: Takayama Y, Clore GM
Abstract
The intra- and intermolecular translocation processes whereby the bi-domain transcription factor Oct1 searches for its specific DNA target site have been investigated by...
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[NMR paper] NMR assignments of the cold-shock protein ribosome-binding factor A (RbfA) from Therm
NMR assignments of the cold-shock protein ribosome-binding factor A (RbfA) from Thermotoga maritima.
Related Articles NMR assignments of the cold-shock protein ribosome-binding factor A (RbfA) from Thermotoga maritima.
J Biomol NMR. 2005 Jan;31(1):73-4
Authors: Grimm SK, Wöhnert J
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[NMR paper] Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation p
Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli.
Related Articles Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli.
J Mol Biol. 2003 Mar 21;327(2):521-36
Authors: Huang YJ, Swapna GV, Rajan PK, Ke H, Xia B, Shukla K, Inouye M, Montelione GT
Ribosome-binding factor A (RbfA) from Escherichia coli is a cold-shock adaptation protein. It is essential for efficient processing of 16S rRNA and is suspected to interact with...
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[NMR paper] Mechanisms for the enhanced thermal stability of a mutant of transcription factor 1 a
Mechanisms for the enhanced thermal stability of a mutant of transcription factor 1 as explained by (1)H, (15)N and (13)C NMR chemical shifts and secondary structure analysis.
Related Articles Mechanisms for the enhanced thermal stability of a mutant of transcription factor 1 as explained by (1)H, (15)N and (13)C NMR chemical shifts and secondary structure analysis.
Biochim Biophys Acta. 2000 Mar 16;1478(1):113-24
Authors: Vu HM, Liu W, Grove A, Geiduschek EP, Kearns DR
A variant of the bacteriophage SPO1-encoded transcription factor 1 (TF1)...
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[NMR paper] New perceptions of transcription factor properties from NMR.
New perceptions of transcription factor properties from NMR.
Related Articles New perceptions of transcription factor properties from NMR.
Biochem Cell Biol. 1998;76(2-3):368-78
Authors: Bagby S, Arrowsmith CH, Ikura M
The complementarity of NMR and X-ray crystallography for biomacromolecular studies has been particularly evident in analysis of transcription factor structures and interactions. While X-ray crystallography can be used to tackle relatively complicated structural problems including multicomponent (three and higher) complexes, NMR...
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[NMR paper] The Aspergillus nidulans transcription factor AlcR forms a stable complex with its ha
The Aspergillus nidulans transcription factor AlcR forms a stable complex with its half-site DNA: a NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The Aspergillus nidulans transcription factor AlcR forms a stable complex with its half-site DNA: a NMR study.
FEBS Lett. 1997 May 19;408(2):235-40
Authors: Cerdan R, Collin D, Lenouvel F, Felenbok B, Guittet E
The Aspergillus nidulans transcription factor AlcR is shown by NMR and gel retardation assay to form a...
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[NMR paper] The Aspergillus nidulans transcription factor AlcR forms a stable complex with its ha
The Aspergillus nidulans transcription factor AlcR forms a stable complex with its half-site DNA: a NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The Aspergillus nidulans transcription factor AlcR forms a stable complex with its half-site DNA: a NMR study.
FEBS Lett. 1997 May 19;408(2):235-40
Authors: Cerdan R, Collin D, Lenouvel F, Felenbok B, Guittet E
The Aspergillus nidulans transcription factor AlcR is shown by NMR and gel retardation assay to form a...
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[NMR paper] A 1H-NMR study of the transcription factor 1 from Bacillus subtilis phage SPO1 by sel
A 1H-NMR study of the transcription factor 1 from Bacillus subtilis phage SPO1 by selective 2H-labeling. Complete assignment and structural analysis of the aromatic resonances for a 22-kDa homodimer.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles A 1H-NMR study of the transcription factor 1 from Bacillus subtilis phage SPO1 by selective 2H-labeling. Complete assignment and structural analysis of the aromatic resonances for a 22-kDa homodimer.
Eur J...