Document Detail


Leucine at codon 428 in the ninth heptad of thyroid hormone receptor beta1 is necessary for interactions with the transcriptional cofactors and functions regardless of dimer formations.
MedLine Citation:
PMID:  12855009     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Structure/function studies of the thyroid hormone receptor (TR) beta(1) have demonstrated that single amino acid substitutions in either position 428 or 429 in the ligand-binding domain (LBD) can alter heterodimerizations and homodimerizations, respectively. A leucine at 428 is located in a highly conserved region corresponding to the putative ninth heptad repeat of a leucine-zipper-like motif in the LBD of TRbeta(1). To investigate how the side chain of amino acids at 428 affect receptor characteristics, gel-shift mobility shift assays and yeast two-hybrid assays were analyzed. The neutral status amino acids such as a leucine (wild-type) or a glutamine at 428 preferred heterodimerization with RXR. Furthermore, a positively charged side chain of amino acids at 428 such as an arginine or a lysine, preserved homodimer formation. Irrespective of charge, ninth heptad mutant receptors did not bind the ligand and were not able to interact with either corepressor or coactivating proteins. Limited trypsinization assays revealed no major conformational change in the ninth heptad mutant receptors. Together, these findings suggested that a leucine at 428 was a critical amino acid for both interaction with the thyroid hormone receptor associated proteins and ligand-independent and -dependent functions regardless of dimer formations.
Authors:
Tsuyoshi Monden; Masanobu Yamada; Sumiyasu Ishii; Takeshi Hosoya; Teturo Satoh; Fredric E Wondisford; Anthony N Hollenberg; Masatomo Mori
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Thyroid : official journal of the American Thyroid Association     Volume:  13     ISSN:  1050-7256     ISO Abbreviation:  Thyroid     Publication Date:  2003 May 
Date Detail:
Created Date:  2003-07-11     Completed Date:  2004-03-26     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  9104317     Medline TA:  Thyroid     Country:  United States    
Other Details:
Languages:  eng     Pagination:  427-35     Citation Subset:  IM    
Affiliation:
First Department of Internal Medicine, Gunma University School of Medicine, Maebashi, Japan. tmonden@showa.gunma-u.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Substitution
Amino Acids / chemistry,  genetics
Animals
Cell Line
Cercopithecus aethiops
Codon / genetics*
Dimerization
Electrophoretic Mobility Shift Assay
Leucine / chemistry,  genetics*
Nuclear Proteins / chemistry,  metabolism
Nuclear Receptor Co-Repressor 1
Protein Conformation
Receptors, Retinoic Acid / chemistry,  metabolism
Recombinant Proteins / chemistry,  genetics,  metabolism
Repressor Proteins / metabolism
Response Elements / genetics
Retinoid X Receptors
Saccharomyces cerevisiae / genetics
Thyroid Hormone Receptors beta / chemistry,  genetics*,  metabolism*
Transcription Factors / chemistry,  metabolism*
Transfection
Two-Hybrid System Techniques
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Codon; 0/Nuclear Proteins; 0/Nuclear Receptor Co-Repressor 1; 0/Receptors, Retinoic Acid; 0/Recombinant Proteins; 0/Repressor Proteins; 0/Retinoid X Receptors; 0/Thyroid Hormone Receptors beta; 0/Transcription Factors; 61-90-5/Leucine

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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