Abstract
A clone corresponding to a thyroid hormone receptor was isolated from a Xenopus laevis cDNA library prepared from folliculated oocytes. The cDNA encodes a protein of 418 amino acid residues with a domain structure, including a putative DNA binding region with two zinc fingers, similar to other members of the v-erbA-related superfamily of receptors. The encoded protein resembles the TR alpha 1-type receptor of the rat. When expressed in COS cells the protein product binds triiodothyronine with a Kd of 0.12 nM. The receptor mediates thyroid-hormone-inducible expression of a reporter gene which includes a thyroid hormone response element in its upstream region.
MeSH Terms
Amino Acid Sequence
Animals
Base Sequence
Cell Line
Cloning, Molecular
Gene Expression
Gene Library
Genes
Kinetics
Molecular Sequence Data
Oocytes/metabolism
Protein Biosynthesis
Protein Conformation
Receptors, Thyroid Hormone/genetics,metabolism
Recombinant Proteins/metabolism
Restriction Mapping
Transcription, Genetic
Transfection
Xenopus laevis
Chemicals
Receptors, Thyroid Hormone
Recombinant Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Brooks A R
Department of Biological Sciences, University of Warwick, Coventry, UK.
Sweeney G
Old R W
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