Document Detail


Characterization and identification of a steroid receptor-binding protein, SRB-RGS.
MedLine Citation:
PMID:  17541154     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We cloned the cDNA of a novel steroid receptor-binding protein, SRB-RGS, which suppressed the estrogen receptor (ER)alpha-mediated and other promoter-driven transcriptional activities. This study revealed the interaction between the full-length SRB-RGS and full-length ERalpha or ERbeta by a coimmunoprecipitation assay. The full-length SRB-RGS and full-length ERalpha interacted in COS-7 cell by a mammalian two-hybrid system. The interaction between intrinsic SRB-RGS and ERs in the nuclear ER extract from the rat uteri was observed by the gel-shift assay. These results strongly suggested that SRB-RGS interacts with ERs bound to DNA (estrogen response element) in the nuclei of the cells. SRB-RGS suppressed very efficiently the ERalpha-, ERbeta-, and ERalpha+ERbeta-mediated transcriptional activities. Green fluorescence of enhanced green fluorescence protein (EGFP)-tagged SRB-RGS was localized both in the nucleus and in the cytoplasm. Intrinsic SRB-RGS was immunostained in the nucleus and the cytoplasm of HeLa cells. The putative SRB-RGS deduced from cDNA sequence was identified by the immunostaining and Western blotting by using the anti-SRB-RGS antibody. Overexpression of SRB-RGS induced the cell death in the HeLa cells. The nucleotide sequence of SRB-RGS cDNA that we cloned previously is identical with that of the newly isolated RGS3 cDNA. SRB-RGS could interact with ERs bound DNA in the nuclei of the cells and suppressed the ERs-mediated transcriptional activities.
Authors:
Mitsunori Ikeda; Satoshi Inoue; Masami Muramatsu; Yohsuke Minatogawa
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biological & pharmaceutical bulletin     Volume:  30     ISSN:  0918-6158     ISO Abbreviation:  Biol. Pharm. Bull.     Publication Date:  2007 Jun 
Date Detail:
Created Date:  2007-06-01     Completed Date:  2007-07-17     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9311984     Medline TA:  Biol Pharm Bull     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  1056-64     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Kawasaki Medical School, Kurashiki, Okayama, Japan. ikeda@bcc.kawasaki-m.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Animals
Base Sequence
Blotting, Western
COS Cells
Cell Death
Cell Nucleus / metabolism
Cercopithecus aethiops
Chloramphenicol O-Acetyltransferase / analysis,  metabolism
Cloning, Molecular
Cytoplasm / metabolism
DNA, Complementary / chemistry,  metabolism
DNA-Binding Proteins / chemistry,  genetics,  metabolism
Electrophoresis, Polyacrylamide Gel
Estrogen Receptor alpha / genetics,  metabolism
Estrogen Receptor beta / genetics,  metabolism
Female
Fluorescent Antibody Technique, Direct
Green Fluorescent Proteins / metabolism
Hela Cells
Humans
Immunohistochemistry
Immunoprecipitation
Microscopy, Confocal
Protein Binding
Rats
Rats, Sprague-Dawley
Receptors, Estrogen / genetics*,  metabolism*
Receptors, Steroid / chemistry,  genetics,  metabolism*
Repressor Proteins / chemistry*,  genetics,  metabolism*
Reverse Transcriptase Polymerase Chain Reaction
Transcription, Genetic
Two-Hybrid System Techniques
Chemical
Reg. No./Substance:
0/DNA, Complementary; 0/DNA-Binding Proteins; 0/Estrogen Receptor alpha; 0/Estrogen Receptor beta; 0/Receptors, Estrogen; 0/Receptors, Steroid; 0/Repressor Proteins; 0/Rgs3 protein, rat; 147336-22-9/Green Fluorescent Proteins; EC 2.3.1.28/Chloramphenicol O-Acetyltransferase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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