scholarly journals Role of the A protein-binding sites in the in vitro transposition of mu DNA. A complex circuit of interactions involving the mu ends and the transpositional enhancer.

1992 ◽  
Vol 267 (28) ◽  
pp. 19963-19970
Author(s):  
R.G. Allison ◽  
G Chaconas
Keyword(s):  
Protein Binding ◽  
Binding Sites ◽  
Protein Binding Sites ◽  
In Vitro Transposition

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 Transcription signals and protein binding sites for sericin gene transcription in vitro

1989 ◽  
Vol 264 (31) ◽  
pp. 18707-18713 ◽  
Author(s):  
K Matsuno ◽  
C C Hui ◽  
S Takiya ◽  
T Suzuki ◽  
K Ueno ◽  
...  
Keyword(s):  
Protein Binding ◽  
Gene Transcription ◽  
Binding Sites ◽  
Protein Binding Sites ◽  
Transcription In Vitro ◽  
Transcription Signals

Characterization of a single strong tissue-specific enhancer downstream from the three human genes encoding placental lactogen

1994 ◽  
Vol 14 (1) ◽  
pp. 93-103
Author(s):  
P Jacquemin ◽  
C Oury ◽  
B Peers ◽  
A Morin ◽  
A Belayew ◽  
...  
Keyword(s):  
Protein Binding ◽  
Binding Sites ◽  
Chromosome 17 ◽  
Placental Lactogen ◽  
Cell Nuclei ◽  
Enhancer Activity ◽  
Protein Binding Sites ◽  
Human Genes ◽  
Genes Encoding

The human genes coding for growth hormone (hGH) and placental lactogen (choriosomatomammotropic hormone [hCS]) are clustered on chromosome 17 in the following order: 5' hGH-N hCS-L hCS-A hGH-V hCS-B 3'. So far, a single placenta-specific enhancer has been identified in the locus, 2 kb downstream from the hCS-B gene, and shown to comprise one in vitro binding site for a nuclear protein. We here provide evidence that the hCS-B enhancer is more complex: (i) protection against DNase I digestion in the 3' flanking region of the hCS-B gene reveals four binding sites (DF-1, DF-2, DF-3, and DF-4) for nuclear proteins from either placental or HeLa cells, and (ii) placenta-specific enhancer activity can be fully exerted in transient expression experiments by a 126-bp fragment comprising the DF-3 and DF-4 protein-binding sites. By dissecting this region, we show that enhancer activity is mediated by a synergy between DF-3 and DF-4. Competitions with various oligonucleotides in footprinting and gel retardation experiments indicate that the same protein or set of proteins, different in HeLa and placenta cell nuclei, interacts with sites DF-2, DF-3, and DF-4. We also studied the regions of the hCS-L and hCS-A genes which are highly similar to the hCS-B enhancer. Although they each present the same four protein-binding sites, they exhibit only minor enhancer activity.

An Improved Method for Identifying Specific DNA-Protein-Binding Sites In Vitro

2017 ◽  
Vol 59 (2-3) ◽  
pp. 59-65
Author(s):  
Liangyan Wang ◽  
Huizhi Lu ◽  
Yunguang Wang ◽  
Su Yang ◽  
Hong Xu ◽  
...  
Keyword(s):  
Protein Binding ◽  
Binding Sites ◽  
Improved Method ◽  
Protein Binding Sites

scholarly journals Analysis of Highly Conserved Regions of the 3’UTR ofMECP2Gene in Patients with Clinical Diagnosis of Rett Syndrome and Other Disorders Associated with Mental Retardation

2008 ◽  
Vol 24 (6) ◽  
pp. 319-324 ◽  
Author(s):  
Mónica Santos ◽  
Jin Yan ◽  
Teresa Temudo ◽  
Guiomar Oliveira ◽  
José Pedro Vieira ◽  
...  
Keyword(s):  
Mental Retardation ◽  
Protein Binding ◽  
Clinical Diagnosis ◽  
Binding Sites ◽  
Pathogenic Role ◽  
Nucleotide Level ◽  
Protein Binding Sites ◽  
Mutation Scanning ◽  
Putative Protein

In this work we explored the role of the 3’UTR of theMECP2gene in patients with clinical diagnosis of RTT and mental retardation; focusing on regions of the 3’UTR with almost 100% conservation at the nucleotide level among mouse and human. By mutation scanning (DOVAM-S technique) theMECP23’UTR of a total of 66 affected females were studied. Five 3’UTR variants in theMECP2were found (c.1461+9G>A, c.1461+98insA, c.2595G>A, c.9961C>G and c.9964delC) in our group of patients. None of the variants found is located in putative protein-binding sites nor predicted to have a pathogenic role. Our data suggest that mutations in this region do not account for a large proportion of the RTT cases without a genetic explanation.

scholarly journals Conserved Structure Modules within the lncRNA SChLAP1 Mediate Protein Recognition Implicated in Aggressive Prostate Cancer

2021 ◽  
Author(s):  
Emily J McFadden ◽  
James P Falese ◽  
Amanda E Hargrove
Keyword(s):  
Prostate Cancer ◽  
Secondary Structure ◽  
Protein Binding ◽  
Binding Sites ◽  
Cancer Metastasis ◽  
Magnesium Concentration ◽  
Purification Method ◽  
Aggressive Prostate Cancer ◽  
Protein Binding Sites

The lncRNA Second Chromosome Locus Associated with Prostate 1 (SChLAP1) was previously identified as a predictive biomarker and driver of aggressive prostate cancer. Recent work suggests that SChLAP1 may bind the SWI/SNF chromatin remodeling complex to promote prostate cancer metastasis, though the exact role of SWI/SNF recognition is debated. To date, there are no detailed biochemical studies of apo SChLAP1 or the SChLAP1:SWI/SNF complex. Herein, we report the first secondary structure model of SChLAP1 utilizing SHAPE-MaP both in vitro and in cellulo. Comparison of the in vitro and in cellulo data via ΔSHAPE identified putative protein binding sites within SChLAP1, specifically to evolutionarily conserved exons of the transcript. We also demonstrate that global SChLAP1 secondary structure is sensitive to both purification method and magnesium concentration. Further, we identified a 3'-fragment of SChLAP1 (SChLAP1Frag) that harbors multiple potential protein binding sites and presents a robustly folded secondary structure, supporting a functional role for this region. This work lays the foundation for future efforts in selective targeting and disruption of the SChLAP1:protein interface and the development of new therapeutic avenues in prostate cancer treatment.

scholarly journals Characterization of a single strong tissue-specific enhancer downstream from the three human genes encoding placental lactogen.

1994 ◽  
Vol 14 (1) ◽  
pp. 93-103 ◽  
Author(s):  
P Jacquemin ◽  
C Oury ◽  
B Peers ◽  
A Morin ◽  
A Belayew ◽  
...  
Keyword(s):  
Protein Binding ◽  
Binding Sites ◽  
Chromosome 17 ◽  
Placental Lactogen ◽  
Cell Nuclei ◽  
Enhancer Activity ◽  
Protein Binding Sites ◽  
Human Genes ◽  
Genes Encoding

The human genes coding for growth hormone (hGH) and placental lactogen (choriosomatomammotropic hormone [hCS]) are clustered on chromosome 17 in the following order: 5' hGH-N hCS-L hCS-A hGH-V hCS-B 3'. So far, a single placenta-specific enhancer has been identified in the locus, 2 kb downstream from the hCS-B gene, and shown to comprise one in vitro binding site for a nuclear protein. We here provide evidence that the hCS-B enhancer is more complex: (i) protection against DNase I digestion in the 3' flanking region of the hCS-B gene reveals four binding sites (DF-1, DF-2, DF-3, and DF-4) for nuclear proteins from either placental or HeLa cells, and (ii) placenta-specific enhancer activity can be fully exerted in transient expression experiments by a 126-bp fragment comprising the DF-3 and DF-4 protein-binding sites. By dissecting this region, we show that enhancer activity is mediated by a synergy between DF-3 and DF-4. Competitions with various oligonucleotides in footprinting and gel retardation experiments indicate that the same protein or set of proteins, different in HeLa and placenta cell nuclei, interacts with sites DF-2, DF-3, and DF-4. We also studied the regions of the hCS-L and hCS-A genes which are highly similar to the hCS-B enhancer. Although they each present the same four protein-binding sites, they exhibit only minor enhancer activity.

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