rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
|
pubmed:dateCreated |
1988-5-4
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pubmed:databankReference |
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pubmed:abstractText |
The complete mRNA sequence of the chicken progesterone receptor (cPR) has been determined. Expression of the cloned cDNA both in vivo and in vitro produces a protein that has the same apparent mol. wt on SDS--polyacrylamide gels as the 'natural' cPR form B (109 kd) as determined by immunoblotting and photoaffinity labelling. When expressed in HeLa or in Cos-1 cells the 'cloned' cPR displays hormone binding characteristics indistinguishable from the 'natural' receptor and, in the presence of progestins, exhibits 'tight nuclear binding'. A protein corresponding in size to the cPR form A (79 kd) could be detected by expressing in vivo and in vitro an N-terminally truncated cPR starting at methionine 128. A protein of the same apparent mol. wt results from internal initiation during in vitro translation. In contrast, such a protein was barely detectable after in vivo expression of the cPR cDNA in Cos-1 cells. These results suggest that form A is generated by an oviduct cell specific process involving either internal initiation of translation and/or proteolysis in the vicinity of methionine-128. The cPR contains two highly conserved regions C and E, a characteristic of the steroid/thyroid hormone receptor supergene family. By expression of a series of cPR deletion mutants, region E could be defined as the hormone binding domain whereas region C is indispensable for the tight nuclear association of the progestin-receptor complex. In the presence of progestins, the cloned cPR efficiently trans-activates transcription from the long terminal repeat region (LTR) of the mouse mammary tumor virus (MMTV). Deletion of the entire N-terminal region A/B or of the hormone binding domain E results in a 100-fold reduction of transcriptional activation. No stimulation of transcription can be detected when the C-terminal deletion extends into region C, indicating that this region is involved in the recognition of the hormone responsive element (HRE) of the MMTV LTR.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3443098-2426697,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3443098-2426779,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3443098-2428599,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/3443098-3011563,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/3443098-7025136
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Dec
|
pubmed:issn |
0261-4189
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
20
|
pubmed:volume |
6
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
3985-94
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:3443098-Amino Acid Sequence,
pubmed-meshheading:3443098-Animals,
pubmed-meshheading:3443098-Base Sequence,
pubmed-meshheading:3443098-Cell Line,
pubmed-meshheading:3443098-Chickens,
pubmed-meshheading:3443098-Chromosome Deletion,
pubmed-meshheading:3443098-Cloning, Molecular,
pubmed-meshheading:3443098-Gene Expression Regulation,
pubmed-meshheading:3443098-Genes,
pubmed-meshheading:3443098-Molecular Sequence Data,
pubmed-meshheading:3443098-Molecular Weight,
pubmed-meshheading:3443098-Protein Biosynthesis,
pubmed-meshheading:3443098-RNA, Messenger,
pubmed-meshheading:3443098-Receptors, Progesterone,
pubmed-meshheading:3443098-Transcription, Genetic
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pubmed:year |
1987
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pubmed:articleTitle |
The chicken progesterone receptor: sequence, expression and functional analysis.
|
pubmed:affiliation |
Laboratoire de Génétique Moléculaire des Eucaryotes du CNRS, Faculté de Médicine, Strasbourg, France.
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pubmed:publicationType |
Journal Article
|