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Molecular cloning and characterization of chicken orphan nuclear
receptor cTR2
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
ID 156332
Author(s) Sanyal, S.; Handschin, C.; Podvinec, M.; Song, K.-H.; Kim, H.-J.; Kim, J.-Y.; Seo, Y.-W.; Kim, S.-A.;
Kwon, H.-B.; Lee, K.; Kim, W.-S.; Meyer, U.A.; Choi, H.-S.
Author(s) at UniBasel Podvinec, Michael;
Year 2003
Title Molecular cloning and characterization of chicken orphan nuclear receptor cTR2
Journal General and Comparative Endocrinology
Volume 132
Number 3
Pages / Article-Number 474-484
Keywords Amino Acid Sequence; Animals; Base Sequence; Chick Embryo; Chickens/*genetics/metabolism;
DNA; Complementary/genetics/isolation & purification; DNA-Binding Proteins/*genetics/metabolism; Gene
Expression Regulation; Developmental; Molecular Sequence Data; Receptors; Estrogen/genetics/metabolism;
Steroid/*genetics/metabolism; Thyroid Hormone/*genetics/metabolism; Tissue Distribution; Trans-Activation
(Genetics)
Orphan nuclear receptors belong to the nuclear receptor superfamily of liganded transcription factors, whose
ligands either do not exist or remain to be identified. We report here the cloning and characterization of the
chicken orphan nuclear receptor, cTR2 (chicken testicular receptor 2). The cTR2 gene encodes a protein of
569 amino acids which shows approximately 72% overall identity with TR2 (NR2C1) and 95% identity in the
DNA-binding domain (DBD). The cTR2 gene is expressed in almost all adult tissues and embryonic stages
examined unlike its mammalian relative TR2, which is specifically expressed in testis. Electrophoretic mobility
shift assays demonstrate that cTR2 binds the canonical direct repeat DNA recognition sequences spaced by
one, four, and five nucleotides (DR1, DR4, and DR5), and in consistence with the results with canonical DNAbinding sequences, cTR2 forms specific DNA-protein complex with chicken phenobarbital response elements
containing DR4 motifs. Both in vitro and in vivo interaction studies demonstrate that cTR2 forms homodimer.
Moreover, transient transfection studies reveal its capability to transactivate canonical DR1, DR4, and DR5
sequences and the constitutive activity of cTR2 is mapped to the N-terminal region of this orphan receptor.
Finally, cTR2 represses transactivation of estrogen receptor in a dose-dependent manner.
ISSN/ISBN 0016-6480
Full Text on edoc
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/12849971