Linked Life Data

2914914

Source:http://linkedlifedata.com/resource/pubmed/id/2914914

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1989-3-21
pubmed:abstractText
The purified estrogen receptor (ER) whether in 9 or 5 S molecular form, binds more than one molecule of the monoclonal antibody JS 34/32 (Redeuilh, G., Moncharmont, B., Secco, C., and Baulieu, E.-E. (1987) J. Biol. Chem. 262, 6969-6975). We now have investigated the effects of controlled trypsin proteolysis and of a dissociating chaotropic salt (NaSCN) on the structure of the estrogen receptor covalently labeled with radioactive tamoxifen aziridine. When the DNA-binding transformed 5S ER was dialyzed against a buffer containing 0.5 M NaSCN, it was converted into a form sedimenting at 3.7 S +/- 0.1 (n = 3). It reverted to the 5 S molecular form when NaSCN was dialyzed away. Fluorographic analysis of both the 5 and 3.7 S ER following SDS-gel electrophoresis revealed one main band corresponding to Mr congruent to 66,000. After limited trypsin treatment of the 5 S ER, tamoxifen aziridine-binding protein sedimented at 4.3 S +/- 0.1 (n = 5), had a Stokes radius of 3.6 nm (calculated Mr = 65,000), and did not bind DNA. The same form was obtained after limited trypsin digestion of the ER bound to DNA-cellulose or to hsp 90 (the nontransformed 8-9 S ER molecular form). This 4.3 S trypsinized ER was reversibly dissociated by NaSCN into a congruent to 3 S +/- 0.1 (n = 3) molecular form. Fluorographic analysis of both the 4.3 and 3 S ER after SDS-gel electrophoresis showed one main radioactive band of Mr congruent to 30,000. Taken together our results suggest that 1) the 5 S ER is a homodimer of two Mr congruent to 66,000 hormone binding subunits which may be released as such from the nontransformed 8-9 S ER, 2) the trypsin digestion products yield two carboxyl-terminal fragments of Mr congruent to 30,000 that remain in the form of a dimer having lost their DNA-binding region, and 3) the trypsin cleavage would occur within the region located between the hormone-binding domain and the DNA-binding domain. These data indicate that the dimerization of the receptor occurs through hydrophobic interaction of its hormone-binding domain but cannot exclude that other part(s) of the receptor may also contribute to the dimer formation. The dimerization may be critically involved in the mechanism by which estradiol-receptor complexes promote change of gene transcription.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2397-400
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Subunit composition of the estrogen receptor. Involvement of the hormone-binding domain in the dimeric state.
pubmed:affiliation
Unité de Recherches sur les Communications Hormonales (Institut National de la Santé et de la Recherche Médicale U. 33), Université Paris-Sud, Bicètre, France.
pubmed:publicationType
Journal Article