Steroid hormone receptor homologs in development

Development ◽  
1989 ◽  
Vol 107 (Supplement) ◽  
pp. 133-140
Author(s):  
Anthony E. Oro ◽  
Kazuhiko Umesono ◽  
Ronald M. Evans
Keyword(s):  
Transcription Factors ◽  
Retinoic Acid ◽  
Hormone Receptor ◽  
Transcriptional Control ◽  
Steroid Hormone ◽  
Steroid Receptor ◽  
Steroid Hormone Receptor ◽  
Functional Domains ◽  
Segmentation Gene ◽  
Thyroid Receptor

The steroid/thyroid receptor superfamily are liganddependent transcription factors which consist of distinct functional domains required for transcriptional control of a network of genes. Members of this superfamily are beginning to be studied for their contribution to embryogenesis. Two human receptors for the vertebrate morphogen retinoic acid have been isolated and further characterized on model promoters. Moreover, the presence of homologs of these receptors in Drosophila reveals that members of this superfamily predate the divergence of the vertebrates and invertebrates. One locus is knirpsrelated (knrl), whose product is closely related to that of the gap segmentation gene knirps (kni). knrl is one of the most diverged steroid receptor-like molecules and displays a spatially restricted blastoderm pattern.

scholarly journals The binding site of a steroid hormone receptor-like protein within the Drosophila Adh adult enhancer is required for high levels of tissue-specific alcohol dehydrogenase expression.

1992 ◽  
Vol 12 (2) ◽  
pp. 661-673 ◽  
Author(s):  
S Ayer ◽  
C Benyajati
Keyword(s):  
Alcohol Dehydrogenase ◽  
Binding Site ◽  
Hormone Receptor ◽  
Steroid Hormone ◽  
Steroid Receptor ◽  
Steroid Hormone Receptor ◽  
Fushi Tarazu ◽  
Enhancer Element ◽  
Tissue Specific ◽  
Adult Tissues

Developmental and tissue-specific transcription from the Adh distal promoter is regulated in part by the Adh adult enhancer, located 450 to 600 bp upstream from the distal RNA start site. We have characterized four proteins (DEP1 to DEP4), present in Drosophila tissue culture cell nuclear extracts, which bind to this enhancer. DEP1 and DEP2 bind to a positive cis-acting element (-492 to -481) and share nucleotide contacts. A small linker replacement deletion mutation, which disrupts the overlapping DEP1- and DEP2-binding sites, reduces Adh distal transcription in an alcohol dehydrogenase (ADH)-expressing cultured cell line, in the adult fat body (the major tissue of ADH expression), as well as in some but not all adult tissues where ADH is normally expressed. This enhancer element contains an imperfect palindromic sequence similar to steroid hormone receptor superfamily response elements. Binding-site screening of a lambda gt11 expression library has identified the steroid receptor superfamily member fushi tarazu factor 1 (FTZ-F1) as a protein that binds to this site. Anti-FTZ-F1 antibodies have identified DEP1 as FTZ-F1. DEP2 also binds to the FTZ-F1 site from the fushi tarazu zebra element, suggesting that DEP2 may also be a steroid receptor superfamily member. Our results raise the possibility that Adh regulation in certain adult tissues involves a hormone-mediated pathway. Because DEP1 (FTZ-F1) and DEP2 contact some of the same nucleotides within the positive cis element, it is unlikely that they can bind simultaneously. Such alternative binding may play a role in the tissue-specific and developmental transcription of Adh.

A novel member of the thyroid/steroid hormone receptor family is encoded by the opposite strand of the rat c-erbA alpha transcriptional unit

1989 ◽  
Vol 9 (3) ◽  
pp. 1128-1136
Author(s):  
M A Lazar ◽  
R A Hodin ◽  
D S Darling ◽  
W W Chin
Keyword(s):  
Retinoic Acid ◽  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Steroid Hormone ◽  
Transcriptional Unit ◽  
Steroid Hormone Receptor ◽  
Genomic Arrangement ◽  
Opposite Strand ◽  
Alpha Gene ◽  
Dna Fragment

A cDNA encoding a novel member of the thyroid/steroid hormone receptor superfamily, called Rev-ErbA alpha, has been isolated from a rat GH3 cell library. Rev-ErbA alpha is an approximately 56-kilodalton protein most similar in structure to the thyroid hormone receptor (c-erbA) and the retinoic acid receptor, but it does not bind either thyroid hormone or retinoic acid. The mRNA encoding Rev-ErbA alpha is present in many tissues and is particularly abundant in skeletal muscle and brown fat. A genomic DNA fragment containing the entire Rev-ErbA alpha cDNA sequence was isolated and characterized. Remarkably, this DNA fragment also contained a portion of the c-erbA alpha gene. r-erbA alpha-1 and r-erbA alpha-2 are alternative splice products of the c-erbA alpha gene and are members of the receptor superfamily. The genes encoding Rev-ErbA alpha and r-erbA alpha-2 overlap, with their coding strands oriented opposite one another. A 269-base-pair segment of the bidirectionally transcribed region is exonic in both the Rev-ErbA alpha and r-erbA alpha-2 genes, resulting in complementary mRNAs. Thus, through alternative splicing and opposite-strand transcription, a single genomic locus codes for three different members of the thyroid/steroid hormone receptor superfamily. Potential implications of this unusual genomic arrangement are discussed.

The binding site of a steroid hormone receptor-like protein within the Drosophila Adh adult enhancer is required for high levels of tissue-specific alcohol dehydrogenase expression

1992 ◽  
Vol 12 (2) ◽  
pp. 661-673
Author(s):  
S Ayer ◽  
C Benyajati
Keyword(s):  
Alcohol Dehydrogenase ◽  
Binding Site ◽  
Hormone Receptor ◽  
Steroid Hormone ◽  
Steroid Receptor ◽  
Steroid Hormone Receptor ◽  
Fushi Tarazu ◽  
Enhancer Element ◽  
Tissue Specific ◽  
Adult Tissues

Developmental and tissue-specific transcription from the Adh distal promoter is regulated in part by the Adh adult enhancer, located 450 to 600 bp upstream from the distal RNA start site. We have characterized four proteins (DEP1 to DEP4), present in Drosophila tissue culture cell nuclear extracts, which bind to this enhancer. DEP1 and DEP2 bind to a positive cis-acting element (-492 to -481) and share nucleotide contacts. A small linker replacement deletion mutation, which disrupts the overlapping DEP1- and DEP2-binding sites, reduces Adh distal transcription in an alcohol dehydrogenase (ADH)-expressing cultured cell line, in the adult fat body (the major tissue of ADH expression), as well as in some but not all adult tissues where ADH is normally expressed. This enhancer element contains an imperfect palindromic sequence similar to steroid hormone receptor superfamily response elements. Binding-site screening of a lambda gt11 expression library has identified the steroid receptor superfamily member fushi tarazu factor 1 (FTZ-F1) as a protein that binds to this site. Anti-FTZ-F1 antibodies have identified DEP1 as FTZ-F1. DEP2 also binds to the FTZ-F1 site from the fushi tarazu zebra element, suggesting that DEP2 may also be a steroid receptor superfamily member. Our results raise the possibility that Adh regulation in certain adult tissues involves a hormone-mediated pathway. Because DEP1 (FTZ-F1) and DEP2 contact some of the same nucleotides within the positive cis element, it is unlikely that they can bind simultaneously. Such alternative binding may play a role in the tissue-specific and developmental transcription of Adh.

scholarly journals A novel member of the thyroid/steroid hormone receptor family is encoded by the opposite strand of the rat c-erbA alpha transcriptional unit.

1989 ◽  
Vol 9 (3) ◽  
pp. 1128-1136 ◽  
Author(s):  
M A Lazar ◽  
R A Hodin ◽  
D S Darling ◽  
W W Chin
Keyword(s):  
Retinoic Acid ◽  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Steroid Hormone ◽  
Transcriptional Unit ◽  
Steroid Hormone Receptor ◽  
Genomic Arrangement ◽  
Opposite Strand ◽  
Alpha Gene ◽  
Dna Fragment

A cDNA encoding a novel member of the thyroid/steroid hormone receptor superfamily, called Rev-ErbA alpha, has been isolated from a rat GH3 cell library. Rev-ErbA alpha is an approximately 56-kilodalton protein most similar in structure to the thyroid hormone receptor (c-erbA) and the retinoic acid receptor, but it does not bind either thyroid hormone or retinoic acid. The mRNA encoding Rev-ErbA alpha is present in many tissues and is particularly abundant in skeletal muscle and brown fat. A genomic DNA fragment containing the entire Rev-ErbA alpha cDNA sequence was isolated and characterized. Remarkably, this DNA fragment also contained a portion of the c-erbA alpha gene. r-erbA alpha-1 and r-erbA alpha-2 are alternative splice products of the c-erbA alpha gene and are members of the receptor superfamily. The genes encoding Rev-ErbA alpha and r-erbA alpha-2 overlap, with their coding strands oriented opposite one another. A 269-base-pair segment of the bidirectionally transcribed region is exonic in both the Rev-ErbA alpha and r-erbA alpha-2 genes, resulting in complementary mRNAs. Thus, through alternative splicing and opposite-strand transcription, a single genomic locus codes for three different members of the thyroid/steroid hormone receptor superfamily. Potential implications of this unusual genomic arrangement are discussed.

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