Basal and parathyroid hormone induced expression of the human 25-hydroxyvitamin D 1α-hydroxylase gene promoter in kidney AOK-B50 cells: role of Sp1, Ets and CCAAT box protein binding sites

2002 ◽  
Vol 34 (8) ◽  
pp. 921-930 ◽  
Author(s):  
Xiu-Hui Gao ◽  
Prem P. Dwivedi ◽  
Sophie Choe ◽  
Frances Alba ◽  
Howard A. Morris ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Protein Binding ◽  
Binding Sites ◽  
Gene Promoter ◽  
Induced Expression ◽  
Protein Binding Sites ◽  
Hydroxyvitamin D ◽  
25 Hydroxyvitamin D ◽  
Ccaat Box

scholarly journals Repression of hsp70 heat shock gene transcription by the suppressor of hairy-wing protein of Drosophila melanogaster.

1991 ◽  
Vol 11 (4) ◽  
pp. 1894-1900 ◽  
Author(s):  
C Holdridge ◽  
D Dorsett
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Protein Binding ◽  
Protein Interactions ◽  
Binding Sites ◽  
Zinc Finger Protein ◽  
Gene Promoter ◽  
Heat Shock Gene ◽  
Protein Binding Sites ◽  
Shock Gene

The suppressor of hairy-wing [su(Hw)] locus of Drosophila melanogaster encodes a zinc finger protein that binds a repeated motif in the gypsy retroposon. Mutations of su(Hw) suppress the phenotypes associated with mutations caused by gypsy insertions. To examine the mechanisms by which su(Hw) alters gene expression, a fragment of gypsy containing multiple su(Hw) protein-binding sites was inserted into various locations in the well-characterized Drosophila hsp70 heat shock gene promoter. We found no evidence for activation of basal hsp70 transcription by su(Hw) protein in cultured Drosophila cells but observed that it can repress heat shock-induced transcription. Repression occurred only when su(Hw) protein-binding sites were positioned between binding sites for proteins required for heat shock transcription. We propose that su(Hw) protein interferes nonspecifically with protein-protein interactions required for heat shock transcription, perhaps sterically, or by altering the ability of DNA to bend or twist.

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.

Repression of hsp70 heat shock gene transcription by the suppressor of hairy-wing protein of Drosophila melanogaster

1991 ◽  
Vol 11 (4) ◽  
pp. 1894-1900
Author(s):  
C Holdridge ◽  
D Dorsett
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Protein Binding ◽  
Protein Interactions ◽  
Binding Sites ◽  
Zinc Finger Protein ◽  
Gene Promoter ◽  
Heat Shock Gene ◽  
Protein Binding Sites ◽  
Shock Gene

The suppressor of hairy-wing [su(Hw)] locus of Drosophila melanogaster encodes a zinc finger protein that binds a repeated motif in the gypsy retroposon. Mutations of su(Hw) suppress the phenotypes associated with mutations caused by gypsy insertions. To examine the mechanisms by which su(Hw) alters gene expression, a fragment of gypsy containing multiple su(Hw) protein-binding sites was inserted into various locations in the well-characterized Drosophila hsp70 heat shock gene promoter. We found no evidence for activation of basal hsp70 transcription by su(Hw) protein in cultured Drosophila cells but observed that it can repress heat shock-induced transcription. Repression occurred only when su(Hw) protein-binding sites were positioned between binding sites for proteins required for heat shock transcription. We propose that su(Hw) protein interferes nonspecifically with protein-protein interactions required for heat shock transcription, perhaps sterically, or by altering the ability of DNA to bend or twist.

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