|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
22
|
|
pubmed:dateCreated |
2001-10-24
|
|
pubmed:abstractText |
Employing a cell-free chromatin transcription system that recapitulates progesterone receptor (PR)-mediated transcription in vivo, we have investigated further the coactivator functions of steroid receptor coactivator-1 (SRC-1) in terms of its functional domains as well as cooperation with other coactivators in PR transactivation. By analyzing wild-type and mutant SRC-1 with liganded PR in the chromatin transcription system in vitro, the basic helix-loop-helix/Per-Arnt-Sim domain, the p300-binding domain, and the carboxyl-terminal region (containing the PR-binding site) of SRC-1 were shown to be important for PR transactivation. Although in context of a synthetic promoter its histone acetyltransferase activity was nonessential for PR-mediated transcription, SRC-1 was observed to act synergistically with p300 to enhance PR transactivation from chromatin. Moreover, SRC-1 and p300 were found to function cooperatively to increase the efficiency of productive transcription initiation and reinitiation. Further analysis of synergism between SRC-1 and p300 revealed an obligatory "sequential" recruitment of SRC-1 and p300 to liganded PR. Efficient recruitment of p300 required the presence of SRC-1. In addition, functional analysis of SRC-2 and SRC-3 coactivators indicated that the SRC family modulated PR transactivation from chromatin by a similar mechanism.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-10051583,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-10368774,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-10381882,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-10449719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-10567538,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-10652267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-10817756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-10934189,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-1517211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-1618161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-3667620,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-7481822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-7979245,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-8446107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-8521507,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-8521509,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-8616895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-8754792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-8799122,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-8945521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-8967953,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-9046951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-9192892,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-9192902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-9223281,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-9267036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-9296499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-9450928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-9575154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11606780-9744281
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/NCOA1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/NCOA3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Receptor Coactivator 1,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Receptor Coactivator 2,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Receptor Coactivator 3,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Progesterone,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sarcosine,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/sarkosyl
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0027-8424
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
23
|
|
pubmed:volume |
98
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
12426-31
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:11606780-Acetyltransferases,
pubmed-meshheading:11606780-Binding Sites,
pubmed-meshheading:11606780-Chromatin,
pubmed-meshheading:11606780-Histone Acetyltransferases,
pubmed-meshheading:11606780-Humans,
pubmed-meshheading:11606780-Nuclear Proteins,
pubmed-meshheading:11606780-Nuclear Receptor Coactivator 1,
pubmed-meshheading:11606780-Nuclear Receptor Coactivator 2,
pubmed-meshheading:11606780-Nuclear Receptor Coactivator 3,
pubmed-meshheading:11606780-Oncogene Proteins,
pubmed-meshheading:11606780-Receptors, Progesterone,
pubmed-meshheading:11606780-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11606780-Sarcosine,
pubmed-meshheading:11606780-Trans-Activators,
pubmed-meshheading:11606780-Transcription, Genetic,
pubmed-meshheading:11606780-Transcription Factors,
pubmed-meshheading:11606780-Transcriptional Activation
|
|
pubmed:year |
2001
|
|
pubmed:articleTitle |
Sequential recruitment of steroid receptor coactivator-1 (SRC-1) and p300 enhances progesterone receptor-dependent initiation and reinitiation of transcription from chromatin.
|
|
pubmed:affiliation |
Department of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
