Linked Life Data

15180993

Source:http://linkedlifedata.com/resource/pubmed/id/15180993

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
2004-8-2
pubmed:abstractText
Thyroid hormone plays important roles in development, differentiation, and metabolic homeostasis by binding to nuclear thyroid hormone receptors, which regulate target gene expression by interacting with DNA response elements and coregulatory proteins. We show that thyroid hormone receptors also are single-stranded RNA binding proteins and that this binding is functionally significant. By using a series of deletion mutants, a novel RNA-binding domain was localized to a 41-amino acid segment of thyroid hormone receptor alpha1 between the second zinc finger and the ligand-binding domain. This RNA-binding domain was necessary and sufficient for thyroid hormone receptor binding to the steroid receptor RNA activator (SRA). Although SRA does not bind directly to steroid receptors, it has been identified as a steroid receptor coactivator, and was thought not to be a coactivator for thyroid hormone receptors. However, transfection studies revealed that SRA enhances thyroid hormone induction of appropriate reporter genes and that the thyroid hormone receptor RNA-binding domain is important for this enhancement. We conclude that thyroid hormone receptors bind RNA through a novel domain and that the interaction of this domain with SRA, and perhaps other RNAs, enhances thyroid hormone receptor function.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33051-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:15180993-Amino Acid Sequence, pubmed-meshheading:15180993-Animals, pubmed-meshheading:15180993-Binding Sites, pubmed-meshheading:15180993-DNA, pubmed-meshheading:15180993-Escherichia coli, pubmed-meshheading:15180993-Gene Deletion, pubmed-meshheading:15180993-Glutathione Transferase, pubmed-meshheading:15180993-Mice, pubmed-meshheading:15180993-Molecular Sequence Data, pubmed-meshheading:15180993-Mutagenesis, pubmed-meshheading:15180993-RNA, pubmed-meshheading:15180993-RNA, Untranslated, pubmed-meshheading:15180993-Rats, pubmed-meshheading:15180993-Recombinant Fusion Proteins, pubmed-meshheading:15180993-Thyroid Hormone Receptors alpha, pubmed-meshheading:15180993-Thyroid Hormone Receptors beta, pubmed-meshheading:15180993-Transcription, Genetic, pubmed-meshheading:15180993-Transfection
pubmed:year
2004
pubmed:articleTitle
An RNA-binding domain in the thyroid hormone receptor enhances transcriptional activation.
pubmed:affiliation
Division of Metabolism, Endocrinology and Diabetes, University of Michigan Medical Center, Ann Arbor, Michigan 48109-0678, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.