scholarly journals The overlapping octamer/TAATGARAT motif is a high-affinity binding site for the cellular transcription factors Oct-1 and Oct-2

1991 ◽  
Vol 277 (2) ◽  
pp. 541-545 ◽  
Author(s):  
C L Dent ◽  
D S Latchman
Keyword(s):  
Single Molecule ◽  
Affinity Binding ◽  
Heterologous Promoter ◽  
High Affinity Binding ◽  
Binding Characteristics ◽  
High Affinity ◽  
Octamer Motif ◽  
High Affinity Binding Site ◽  
Simplex Virus ◽  
Cellular Transcription

The octamer motif in cellular promoters and the related TAATGARAT element in the herpes simplex virus (HSV) immediate-early promoters can both bind cellular octamer-binding proteins. The overlapping octamer/TAATGARAT elements (consensus ATGCTAATGARAT) found in the HSV-1 IE1 promoter thus represent a composite motif, each portion of which can independently bind octamer-binding protein. By comparing the binding characteristics of this composite motif with its individual elements, we show that it binds a single molecule of either Oct-1 or Oct-2 with much higher affinity than does either an octamer or TAATGARAT motif alone. This strong binding allows this element to direct a much higher level of gene expression when linked to a heterologous promoter than that observed with each of its individual components.

scholarly journals High-affinity binding site for a specific nuclear protein in the human IgM gene

Nature ◽  
1985 ◽  
Vol 315 (6016) ◽  
pp. 254-254
Author(s):  
L. Hennighausen ◽  
U. Siebenlist ◽  
D. Danner ◽  
P. Leder ◽  
D. Rawlins ◽  
...  
Keyword(s):  
Binding Site ◽  
Nuclear Protein ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity ◽  
High Affinity Binding Site ◽  
Specific Nuclear Protein

Regulatory effect of cholecystokinin on subsequent insulin binding to pancreatic acini

1990 ◽  
Vol 258 (4) ◽  
pp. E562-E568
Author(s):  
Y. Okabayashi ◽  
M. Otsuki ◽  
T. Nakamura ◽  
M. Koide ◽  
H. Hasegawa ◽  
...  
Keyword(s):  
Binding Site ◽  
Insulin Binding ◽  
Pancreatic Acinar Cells ◽  
Affinity Binding ◽  
Regulatory Effect ◽  
Pancreatic Acini ◽  
High Affinity Binding ◽  
Receptor Affinity ◽  
High Affinity ◽  
High Affinity Binding Site

We investigated the regulatory effect of cholecystokinin (CCK) on subsequent insulin binding to pancreatic acinar cells. Rat isolated acini were preincubated with various concentrations of CCK octapeptide (CCK-8) at 37 degrees C. Acini were then washed, resuspended in the binding buffer, and incubated with 8.3 pM 125I-labeled insulin for 60 min at 37 degrees C. Pretreatment with CCK-8 caused inhibition of subsequent 125I-insulin binding that was time and concentration dependent. Significant inhibition was observed with 3 pM CCK-8. Computer analysis of the competition-inhibition study with a nonlinear least-squares curve-fitting program revealed that CCK-8 pretreatment of acini reduced the receptor affinity of the high-affinity binding site. This inhibitory action of CCK-8 was not due to the alteration in degradation or internalization of the tracer. When acini were pretreated with 100 pM CCK-8 for 120 min at 4 degrees C, a reduction in the receptor affinity of the high-affinity binding site was also observed. In pancreatic membrane prepared from acini preincubated with 100 pM CCK-8 for 120 min at 37 degrees C, displacement of 125I-insulin (83 pM) by unlabeled insulin (24 degrees C, 1 h) revealed that CCK-8 inhibited 125I-insulin binding by altering the receptor affinity of the high-affinity binding site. In acinar preparations the inhibitory effect of CCK-8 on 125I-insulin binding was abolished when acini were preincubated with CCK-8 and CCK receptor antagonist L 374718 at 37 degrees C.(ABSTRACT TRUNCATED AT 250 WORDS)

A gonadotropin-releasing hormone type neuropeptide with a high affinity binding site for copper(ii) and nickel(ii)

Metallomics ◽  
2019 ◽  
Vol 11 (2) ◽  
pp. 404-414 ◽  
Author(s):  
Kevin K. Tran ◽  
Bhawantha M. Jayawardena ◽  
Maurice R. Elphick ◽  
Christopher E. Jones
Keyword(s):  
Binding Site ◽  
Gonadotropin Releasing Hormone ◽  
Affinity Binding ◽  
Asterias Rubens ◽  
High Affinity Binding ◽  
Releasing Hormone ◽  
High Affinity ◽  
Evolutionarily Conserved ◽  
High Affinity Site ◽  
High Affinity Binding Site

Gonadotropin releasing hormone from Asterias rubens binds Cu(ii) in a nitrogen-rich, high-affinity site. Cu(ii)-binding is an evolutionarily conserved feature of GnRH-type neuropeptides.

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