The presence of sequence-specific protein binding sites correlate with replication activity and matrix binding in a 1.7 Kb-long DNA fragment of the chicken ∝-globin gene domain

1991 ◽  
Vol 179 (1) ◽  
pp. 512-519 ◽  
Author(s):  
C.V. de Moura Gallo ◽  
Y.S. Vassetzky ◽  
F.Recillas Targa ◽  
G.P. Georgive ◽  
K. Scherrer ◽  
...  
Keyword(s):  
Protein Binding ◽  
Binding Sites ◽  
Globin Gene ◽  
Specific Protein ◽  
Protein Binding Sites ◽  
Dna Fragment ◽  
Globin Gene Domain ◽  
Replication Activity

EVALUATION OF TISSUE STEROID BINDING IN VITRO

1971 ◽  
Vol 68 (1_Suppl) ◽  
pp. S223-S246 ◽  
Author(s):  
C. R. Wira ◽  
H. Rochefort ◽  
E. E. Baulieu
Keyword(s):  
Protein Binding ◽  
Binding Sites ◽  
Experimental System ◽  
Specific Protein ◽  
Coupling Mechanism ◽  
Target Tissue ◽  
Protein Binding Sites ◽  
Definition Of ◽  
Hormone Specificity

ABSTRACT The definition of a RECEPTOR* in terms of a receptive site, an executive site and a coupling mechanism, is followed by a general consideration of four binding criteria, which include hormone specificity, tissue specificity, high affinity and saturation, essential for distinguishing between specific and nonspecific binding. Experimental approaches are proposed for choosing an experimental system (either organized or soluble) and detecting the presence of protein binding sites. Techniques are then presented for evaluating the specific protein binding sites (receptors) in terms of the four criteria. This is followed by a brief consideration of how receptors may be located in cells and characterized when extracted. Finally various examples of oestrogen, androgen, progestagen, glucocorticoid and mineralocorticoid binding to their respective target tissues are presented, to illustrate how researchers have identified specific corticoid and mineralocorticoid binding in their respective target tissue receptors.

scholarly journals Maximal Activity of an Erythroid-specific Enhancer Requires the Presence of Specific Protein Binding Sites in Linked Promoters

1998 ◽  
Vol 273 (22) ◽  
pp. 13593-13598 ◽  
Author(s):  
Persis J. Amrolia ◽  
Wesley Gabbard ◽  
John M. Cunningham ◽  
Stephen M. Jane
Keyword(s):  
Protein Binding ◽  
Binding Sites ◽  
Maximal Activity ◽  
Specific Protein ◽  
Protein Binding Sites

scholarly journals Identification of regulatory sequences and protein-binding sites in the liver-type promoter of a gene encoding 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.

1991 ◽  
Vol 11 (2) ◽  
pp. 1099-1106 ◽  
Author(s):  
F P Lemaigre ◽  
S M Durviaux ◽  
G G Rousseau
Keyword(s):  
Protein Binding ◽  
Binding Sites ◽  
Specific Protein ◽  
Regulatory Sequences ◽  
Alternative Promoters ◽  
Gene Encoding ◽  
Protein Binding Sites ◽  
Cis Acting ◽  
Dnase I Footprinting ◽  
Nuclear Extracts

The liver-type and muscle-type isozymes of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase are encoded by one gene that uses two alternative promoters. We have identified cis-acting sequences and protein-binding sites on the liver-type promoter. Transfection assays with deleted promoters showed that maximal promoter activity is contained within 360 bp upstream of the cap site. DNase I footprinting experiments with liver and spleen nuclear extracts and with purified proteins revealed several protein-binding sites in this region. These included four binding sites for nuclear factor I, one site that contains an octamer consensus but showed a liver-specific footprint pattern, two liver-specific protein-binding sites, and one poly(dG)-containing binding site. Transfection of cells of hepatic origin suggested that all these sites except one are involved in transcriptional regulation. The region between -360 and -2663 contained an element that functioned as a silencer in a nonhepatic cell line. We conclude that in liver transcription from the liver-type promoter of the 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene is controlled by ubiquitous and tissue-specific factors and involves activating and derepressing mechanisms.

scholarly journals Organization of the 3′-boundary of the chicken α globin gene domain and characterization of a CR 1-specific protein binding site

1990 ◽  
Vol 18 (3) ◽  
pp. 401-409 ◽  
Author(s):  
Gabriel Farache ◽  
Sergey V. Razin ◽  
Félix Recillas Targa ◽  
Klaus Scherrer
Keyword(s):  
Protein Binding ◽  
Binding Site ◽  
Globin Gene ◽  
Specific Protein ◽  
Protein Binding Site ◽  
Globin Gene Domain

scholarly journals Protein-binding sites within the 5' DNase I-hypersensitive region of the chicken alpha D-globin gene.

1987 ◽  
Vol 7 (6) ◽  
pp. 2059-2069 ◽  
Author(s):  
B Kemper ◽  
P D Jackson ◽  
G Felsenfeld
Keyword(s):  
Protein Binding ◽  
Binding Sites ◽  
Globin Gene ◽  
Regulatory Elements ◽  
Dnase I ◽  
Specific Factor ◽  
Mobility Shift ◽  
Protein Binding Sites ◽  
Dnase I Footprinting ◽  
Flanking Region

We mapped at high resolution and as a function of development the hypersensitive domain in the 5'-flanking region of the chicken alpha D-globin gene and determined the specific protein-binding sites within the domain. The domain extends from -130 to +80 nucleotides (nt) relative to the cap site. DNase I footprinting within intact embryonic erythrocyte nuclei revealed a strongly protected area from -71 to -52 nt. The same area was weakly protected in adult nuclei. A factor was present in extracts of erythrocyte nuclei from both embryos and adults that protected the sequence AAGATAAGG (-63 to -55 nt) in DNase I footprinting experiments; at higher concentrations of extract, sequences immediately adjacent (-73 to -64 and -53 to -38) were also protected. The same pattern of binding was revealed by gel mobility shift assays. The identical AAGATAAGG sequence is found in the 5'-flanking region of the beta rho gene; it competed for binding of the alpha D-specific factor, suggesting that regulatory elements are shared.

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