Proteins associated with untransformed estrogen receptor in vitro. Perturbation of hydrophobic interactions induces alterations in quaternary structure and exposure of the DNA-binding site

Biochemistry ◽  
1987 ◽  
Vol 26 (18) ◽  
pp. 5608-5616 ◽  
Author(s):  
T. William Hutchens ◽  
Chee Ming Li ◽  
Paige K. Besch
Keyword(s):  
Estrogen Receptor ◽  
Dna Binding ◽  
Binding Site ◽  
Quaternary Structure ◽  
Hydrophobic Interactions ◽  
Dna Binding Site

scholarly journals Structural determinants of DNA recognition by plant MADS-domain transcription factors

2013 ◽  
Vol 42 (4) ◽  
pp. 2138-2146 ◽  
Author(s):  
Jose M. Muiño ◽  
Cezary Smaczniak ◽  
Gerco C. Angenent ◽  
Kerstin Kaufmann ◽  
Aalt D.J. van Dijk
Keyword(s):  
Transcription Factors ◽  
Dna Binding ◽  
Binding Site ◽  
Structural Characteristics ◽  
Binding Specificity ◽  
Structural Motif ◽  
Dna Binding Specificity ◽  
Dna Binding Site ◽  
Carg Box

Abstract Plant MADS-domain transcription factors act as key regulators of many developmental processes. Despite the wealth of information that exists about these factors, the mechanisms by which they recognize their cognate DNA-binding site, called CArG-box (consensus CCW6GG), and how different MADS-domain proteins achieve DNA-binding specificity, are still largely unknown. We used information from in vivo ChIP-seq experiments, in vitro DNA-binding data and evolutionary conservation to address these important questions. We found that structural characteristics of the DNA play an important role in the DNA binding of plant MADS-domain proteins. The central region of the CArG-box largely resembles a structural motif called ‘A-tract’, which is characterized by a narrow minor groove and may assist bending of the DNA by MADS-domain proteins. Periodically spaced A-tracts outside the CArG-box suggest additional roles for this structure in the process of DNA binding of these transcription factors. Structural characteristics of the CArG-box not only play an important role in DNA-binding site recognition of MADS-domain proteins, but also partly explain differences in DNA-binding specificity of different members of this transcription factor family and their heteromeric complexes.

scholarly journals CT-1 and Oct-2 DNA-binding site specificity is regulated in vitro by different kinases

1996 ◽  
Vol 317 (3) ◽  
pp. 959-959
Author(s):  
S. J. GRENFELL ◽  
D. S. LATCHMAN ◽  
N. S. B. THOMAS
Keyword(s):  
Dna Binding ◽  
Binding Site ◽  
Site Specificity ◽  
Dna Binding Site

scholarly journals Properties of a high-affinity DNA binding site for estrogen receptor.

1988 ◽  
Vol 85 (4) ◽  
pp. 1038-1042 ◽  
Author(s):  
F. V. Peale ◽  
L. B. Ludwig ◽  
S. Zain ◽  
R. Hilf ◽  
R. A. Bambara
Keyword(s):  
Estrogen Receptor ◽  
Dna Binding ◽  
Binding Site ◽  
High Affinity ◽  
Dna Binding Site

scholarly journals Identification and Functional Characterization of a High-Affinity Bel-1 DNA Binding Site Located in the Human Foamy Virus Internal Promoter

1998 ◽  
Vol 72 (1) ◽  
pp. 504-511 ◽  
Author(s):  
Yibin Kang ◽  
Wade S. Blair ◽  
Bryan R. Cullen
Keyword(s):  
Dna Binding ◽  
Binding Site ◽  
Foamy Virus ◽  
Promoter Element ◽  
Internal Promoter ◽  
Dna Binding Site ◽  
Foamy Viruses ◽  
Ltr Promoter

ABSTRACT The transcription of genes carried by primate foamy viruses is dependent on two distinct promoter elements. These are the long terminal repeat (LTR) promoter, which regulates expression of the viral structural proteins, and a second internal promoter, located towards the 3′ end of the env gene, that directs expression of the viral auxiliary proteins. One of these auxiliary proteins is a potent transcriptional transactivator, termed Bel-1 in human foamy virus (HFV) and Tas or Taf in the related simian foamy viruses, that is critical for foamy virus replication. Previously, it has been demonstrated that the LTR promoter element of HFV contains a DNA binding site for Bel-1 that is critical for transcriptional activation (F. He, W. S. Blair, J. Fukushima, and B. R. Cullen, J. Virol. 70:3902–3908, 1996). Here, we extended this earlier work by using methylation interference analysis to identify and characterize the Bel-1 DNA binding sites located in the HFV LTR and internal promoter elements. Based on these data, we propose a minimal, 25-bp DNA binding site for Bel-1, derived from the HFV internal promoter element, and show that this short DNA sequence mediates efficient Bel-1 binding both in vitro and in vivo. We further demonstrate that, as determined by both in vitro and in vivo assays, the Bel-1 target site located within the HFV internal promoter binds Bel-1 with a significantly higher affinity than the cap-proximal Bel-1 target site located in the LTR promoter. This result may provide a mechanistic explanation for the observation that the internal promoter is activated significantly earlier than the LTR promoter during the foamy virus life cycle.

scholarly journals Identification of the DNA binding element of the human ZNF300 protein

2008 ◽  
Vol 13 (3) ◽  
Author(s):  
Hongling Qiu ◽  
Lu Xue ◽  
Li Gao ◽  
Huanjie Shao ◽  
Di Wang ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Site ◽  
Electrophoretic Mobility ◽  
Nuclear Protein ◽  
Transcriptional Regulator ◽  
Mobility Shift ◽  
Dna Binding Site ◽  
Specific Manner ◽  
Electrophoretic Mobility Shift Assays

AbstractThe human ZNF300 gene is a member of the KRAB/C2H2 zinc finger gene family, the members of which are known to be involved in various developmental and pathological processes. Here, we show that the ZNF300 gene encodes a 68-kDa nuclear protein that binds DNA in a sequence-specific manner. The ZNF300 DNA binding site, C(t/a)GGGGG(c/g)G, was defined via a random oligonucleotide selection assay, and the DNA binding site was further confirmed by electrophoretic mobility shift assays. A potential ZNF300 binding site was found in the promoter region of the human IL-2Rβ gene. The results of electrophoretic mobility shift assays indicated that ZNF300 bound to the ZNF300 binding site in the IL-2Rβ promoter in vitro. Transient co-transfection assays showed that ZNF300 could activate the IL-2Rβ promoter, and that the activation was abrogated by the mutation of residues in the ZNF300 binding site. Identifying the DNA binding site and characterizing the transcriptional regulation property of ZNF300 would provide critical insights into its potential as a transcriptional regulator.

scholarly journals Determinants for DNA-binding site recognition by the glucocorticoid receptor.

1992 ◽  
Vol 267 (35) ◽  
pp. 24941-24947
Author(s):  
J Zilliacus ◽  
A.P. Wright ◽  
U Norinder ◽  
J.A. Gustafsson ◽  
J Carlstedt-Duke
Keyword(s):  
Dna Binding ◽  
Glucocorticoid Receptor ◽  
Binding Site ◽  
Dna Binding Site ◽  
Site Recognition
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