Publication Date:
1995-11-24
Description:
A yeast two-hybrid system was used to identify a protein that interacts with and enhances the human progesterone receptor (hPR) transcriptional activity without altering the basal activity of the promoter. Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). Coexpression of SRC-1 reversed the ability of the estrogen receptor to squelch activation by hPR. Also, the amino terminal truncated form of SRC-1 acted as a dominant-negative repressor. Together, these results indicate that SRC-1 encodes a coactivator that is required for full transcriptional activity of the steroid receptor superfamily.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Onate, S A -- Tsai, S Y -- Tsai, M J -- O'Malley, B W -- HD08188/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 24;270(5240):1354-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481822" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Base Sequence
;
Cyclic AMP Response Element-Binding Protein/metabolism
;
Gene Expression
;
HeLa Cells
;
Histone Acetyltransferases
;
Hormone Antagonists/metabolism/pharmacology
;
Humans
;
Mifepristone/metabolism/pharmacology
;
Molecular Sequence Data
;
Nuclear Receptor Coactivator 1
;
Promegestone/pharmacology
;
Receptors, Progesterone/*metabolism
;
Receptors, Steroid/*metabolism
;
Recombinant Fusion Proteins/metabolism
;
Trans-Activators/*metabolism
;
Transcription Factors/*chemistry/genetics/*metabolism
;
*Transcriptional Activation
;
Transfection
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
