Transcriptional control by estradiol receptor

1995 ◽  
Vol 8 (1-2) ◽  
pp. 162-163
Author(s):  
Giovanni Alfredo Puca ◽  
Nicola Medici ◽  
Ciro Abbondanza ◽  
Ignazio Armetta ◽  
Vincenzo Nigro ◽  
...  
Keyword(s):  
Transcriptional Control ◽  
Estradiol Receptor

Nutrient-regulated gene expression in eukaryotes

2006 ◽  
Vol 73 ◽  
pp. 85-96 ◽  
Author(s):  
Richard J. Reece ◽  
Laila Beynon ◽  
Stacey Holden ◽  
Amanda D. Hughes ◽  
Karine Rébora ◽  
...  
Keyword(s):  
Gene Expression ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcriptional Control ◽  
Direct Interaction ◽  
Signalling Pathways ◽  
A Cell ◽  
One Step ◽  
Higher Eukaryotes ◽  
Regulated Gene Expression

The recognition of changes in environmental conditions, and the ability to adapt to these changes, is essential for the viability of cells. There are numerous well characterized systems by which the presence or absence of an individual metabolite may be recognized by a cell. However, the recognition of a metabolite is just one step in a process that often results in changes in the expression of whole sets of genes required to respond to that metabolite. In higher eukaryotes, the signalling pathway between metabolite recognition and transcriptional control can be complex. Recent evidence from the relatively simple eukaryote yeast suggests that complex signalling pathways may be circumvented through the direct interaction between individual metabolites and regulators of RNA polymerase II-mediated transcription. Biochemical and structural analyses are beginning to unravel these elegant genetic control elements.

THE BIOSYNTHETIC SEQUENCE OF THE VARIOUS FORMS OF CYTOPLASMIC ESTRADIOL RECEPTOR

1974 ◽  
Vol 77 (1_Suppl) ◽  
pp. S147
Author(s):  
P. I. Szendro ◽  
M. Little ◽  
P. W. Jungblut
Keyword(s):  
Estradiol Receptor

The extractability of estradiol receptor from unterine nuclei is independent of in-vivo exposure to estradiol

1986 ◽  
Vol 113 (1_Suppl) ◽  
pp. S150-S151 ◽  
Author(s):  
P. W. JUNGBLUT ◽  
E. KALLWEIT ◽  
P. I. SZENDRO
Keyword(s):  
Estradiol Receptor

MicroRNAs regulate aldosterone signaling by post-transcriptional control of mineralocorticoid receptor expression

2019 ◽  
Author(s):  
Thi-An Vu ◽  
Ingrid Lema ◽  
Jerome Bouligand ◽  
Laetitia Martinerie ◽  
Marc Lombes ◽  
...  
Keyword(s):  
Mineralocorticoid Receptor ◽  
Transcriptional Control ◽  
Receptor Expression

Post-Transcriptional Regulation of Cardiac Sarcomere Protein Titin Through 3’ Untranslated Regions

2013 ◽  
Vol 9 ◽  
Author(s):  
Tara A Shrout
Keyword(s):  
Gene Expression ◽  
Transcriptional Control ◽  
Striated Muscle ◽  
Binding Capacity ◽  
Structural Features ◽  
Neonatal Rat ◽  
Regulatory Control ◽  
Untranslated Regions ◽  
Luciferase Reporter ◽  
Regulatory Effects

Titin is the largest known protein in the human body, and forms the backbone of all striated muscle sarcomeres. The elastic nature of titin is an important component of muscle compliance and functionality. A significant amount of energy is expended to synthesize titin, thus we postulate that titin gene expression is under strict regulatory control in order to conserve cellular resources. In general, gene expression is mediated in part by post-transcriptional control elements located within the 5’ and 3’ untranslated regions (UTRs) of mature mRNA. The 3’UTR in particular contains structural features that affect binding capacity to other RNA components, such as MicroRNA, which control mRNA localization, translation, and degradation. The degree and significance of the regulatory effects mediated by two determined variants of titin’s 3’ UTR were evaluated in Neonatal Rat Ventricular Myocyte and Human Embryonic Kidney cell lines. Recombinant plasmids to transfect these cells lines were engineered by insertion of the variant titin 3’UTR 431- and 1047-base pairs sequences into luciferase reporter vectors. Expression due to an unaltered reporter vector served as the control. Quantitative changes in luciferase activity due to the recombinants proportionally represented the effect titin’s respective 3’UTR conferred on downstream post-transcriptional expression relative to the control. The effect due to titin’s shorter 3’UTR sequence was inconclusive; however, results illustrated that titin’s longer 3’UTR sequence caused a 35 percent decrease in protein expression. Secondary structural analysis of the two sequences revealed differential folding patterns that affect the stability and degree of MicroRNA-binding within titin’s variant 3’UTR sequences.

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