Purification and biochemical characterization of the promoter-specific transcription factor, Sp1

Science ◽  
1986 ◽  
Vol 234 (4772) ◽  
pp. 47-52 ◽  
Author(s):  
M. Briggs ◽  
J. Kadonaga ◽  
S. Bell ◽  
R Tjian
Keyword(s):  
Transcription Factor ◽  
Biochemical Characterization ◽  
Specific Transcription Factor ◽  
Transcription Factor Sp1

Characterization of a spliced variant of human IRF-3 promoter and its regulation by the transcription factor Sp1

2012 ◽  
Vol 39 (6) ◽  
pp. 6987-6993 ◽  
Author(s):  
Wei Ren ◽  
Liang-Hua Zhu ◽  
Hua-Guo Xu ◽  
Rui Jin ◽  
Guo-Ping Zhou
Keyword(s):  
Transcription Factor ◽  
Transcription Factor Sp1 ◽  
Spliced Variant

scholarly journals Molecular Characterization of Saccharomyces cerevisiae TFIID

2002 ◽  
Vol 22 (16) ◽  
pp. 6000-6013 ◽  
Author(s):  
Steven L. Sanders ◽  
Krassimira A. Garbett ◽  
P. Anthony Weil
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Transcription Factor ◽  
Molecular Mass ◽  
Molecular Characterization ◽  
Biochemical Characterization ◽  
Gel Filtration ◽  
Calculated Molecular Mass ◽  
General Transcription Factor

ABSTRACT We previously defined Saccharomyces cerevisiae TFIID as a 15-subunit complex comprised of the TATA binding protein (TBP) and 14 distinct TBP-associated factors (TAFs). In this report we give a detailed biochemical characterization of this general transcription factor. We have shown that yeast TFIID efficiently mediates both basal and activator-dependent transcription in vitro and displays TATA box binding activity that is functionally distinct from that of TBP. Analyses of the stoichiometry of TFIID subunits indicated that several TAFs are present at more than 1 copy per TFIID complex. This conclusion was further supported by coimmunoprecipitation experiments with a systematic family of (pseudo)diploid yeast strains that expressed epitope-tagged and untagged alleles of the genes encoding TFIID subunits. Based on these data, we calculated a native molecular mass for monomeric TFIID. Purified TFIID behaved in a fashion consistent with this calculated molecular mass in both gel filtration and rate-zonal sedimentation experiments. Quite surprisingly, although the TAF subunits of TFIID cofractionated as a single complex, TBP did not comigrate with the TAFs during either gel filtration chromatography or rate-zonal sedimentation, suggesting that TBP has the ability to dynamically associate with the TFIID TAFs. The results of direct biochemical exchange experiments confirmed this hypothesis. Together, our results represent a concise molecular characterization of the general transcription factor TFIID from S. cerevisiae.

Molecular and SNP characterization of two genome specific transcription factor genes GhMyb8 and GhMyb10 in cotton species

Euphytica ◽  
2007 ◽  
Vol 159 (1-2) ◽  
pp. 259-273 ◽  
Author(s):  
Chuan-Yu Hsu ◽  
Chuanfu An ◽  
Sukumar Saha ◽  
Din-Pow Ma ◽  
Johnie N. Jenkins ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Specific Transcription Factor ◽  
Cotton Species ◽  
Transcription Factor Genes

Characterization of the human SLC22A18 gene promoter and its regulation by the transcription factor Sp1

Gene ◽  
2009 ◽  
Vol 429 (1-2) ◽  
pp. 37-43 ◽  
Author(s):  
Abdullah Mahmood Ali ◽  
Vineeta Bajaj ◽  
K.S. Gopinath ◽  
Arun Kumar
Keyword(s):  
Transcription Factor ◽  
Gene Promoter ◽  
Transcription Factor Sp1

scholarly journals Purification and characterization of thyroid transcription factor 2

1994 ◽  
Vol 304 (3) ◽  
pp. 981-985 ◽  
Author(s):  
D Civitareale ◽  
A Saiardi ◽  
P Falasca
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Biochemical Characterization ◽  
Binding Protein ◽  
Thyroid Tissue ◽  
Dna Binding Protein ◽  
Purification And Characterization ◽  
Thyroid Transcription Factor

Thyroid transcription factor 2 binds to the promoters of both thyroglobulin and thyroperoxidase genes, two markers of thyroid tissue differentiation, and its binding modulates the activity of both promoters. In this paper we describe the purification of thyroid transcription factor 2 essentially to homogeneity and demonstrate that it is a thyroid-specific DNA-binding protein. Furthermore, we provide a biochemical characterization suggesting that thyroid transcription factor 2 binds to DNA as a dimer and that it is a zinc-finger DNA-binding protein regulated in vitro by the redox state.

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