Cloning and chromosome mapping of human retinoid X receptor ?: selective amino acid sequence conservation of a nuclear hormone receptor in mammals

1993 ◽  
Vol 90 (5) ◽  
Author(s):  
K. Fleischhauer ◽  
O.W. McBride ◽  
J.P. DiSanto ◽  
K. Ozato ◽  
S.Y. Yang
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Hormone Receptor ◽  
Chromosome Mapping ◽  
Nuclear Hormone Receptor ◽  
Retinoid X Receptor ◽  
Sequence Conservation ◽  
Amino Acid Sequence Conservation

scholarly journals Nephrocystin

2000 ◽  
Vol 11 (2) ◽  
pp. 270-282
Author(s):  
EDGAR OTTO ◽  
ANDREAS KISPERT ◽  
SILVIA SCHÄTZLE ◽  
BIRGIT LESCHER ◽  
CORNELIA RENSING ◽  
...  
Keyword(s):  
Amino Acid ◽  
Caenorhabditis Elegans ◽  
Amino Acid Sequence ◽  
Protein Interaction ◽  
Tissue Expression ◽  
Sequence Conservation ◽  
Cystic Kidney ◽  
Protein Protein Interaction ◽  
Amino Acid Sequence Conservation

Juvenile nephronophthisis, an autosomal recessive cystic kidney disease, is the primary genetic cause for chronic renal failure in children. The gene (NPHP 1) for nephronophthisis type 1 has recently been identified. Its gene product, nephrocystin, is a novel protein of unknown function, which contains a src-homology 3 domain. To study tissue expression and analyze amino acid sequence conservation of nephrocystin, the full-length murine Nphp 1 cDNA sequence was obtained and Northern and in situ hybridization analyses were performed for extensive expression studies. The results demonstrate widespread but relatively weak NPHP 1 expression in the human adult. In the adult mouse there is strong expression in testis. This expression occurs specifically in cell stages of the first meiotic division and thereafter. In situ hybridization to whole mouse embryos demonstrated widespread and uniform expression at all developmental stages. Amino acid sequence conservation studies in human, mouse, and Caenorhabditis elegans show that in nephrocystin the src-homology 3 domain is embedded in a novel context of other putative domains of protein-protein interaction, such as coiled-coil and E-rich domains. It is concluded that for multiple putative protein-protein interaction domains of nephrocystin, sequence conservation dates back at least to Caenorhabditis elegans. The previously described discrepancy between widespread tissue expression and the restriction of symptoms to the kidney has now been confirmed by an in-depth expression study.

scholarly journals Amino acid sequence conservation of the algesic fragment of myelin basic protein is required for its interaction with CDK 5 and function in pain

FEBS Journal ◽  
2018 ◽  
Vol 285 (18) ◽  
pp. 3485-3502
Author(s):  
Andrei V. Chernov ◽  
Albert G. Remacle ◽  
Swathi K. Hullugundi ◽  
Piotr Cieplak ◽  
Mila Angert ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Sequence Conservation ◽  
And Function ◽  
Amino Acid Sequence Conservation

Dynamic Behavior of an Intrinsically Unstructured Linker Domain Is Conserved in the Face of Negligible Amino Acid Sequence Conservation

2007 ◽  
Vol 65 (3) ◽  
pp. 277-288 ◽  
Author(s):  
Gary W. Daughdrill ◽  
Pranesh Narayanaswami ◽  
Sara H. Gilmore ◽  
Agniezka Belczyk ◽  
Celeste J. Brown
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Dynamic Behavior ◽  
Sequence Conservation ◽  
The Face ◽  
Linker Domain ◽  
Amino Acid Sequence Conservation

scholarly journals A nuclear hormone receptor corepressor mediates transcriptional silencing by receptors with distinct repression domains.

1996 ◽  
Vol 16 (10) ◽  
pp. 5458-5465 ◽  
Author(s):  
I Zamir ◽  
H P Harding ◽  
G B Atkins ◽  
A Hörlein ◽  
C K Glass ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nuclear Receptors ◽  
Hormone Receptor ◽  
Transcriptional Repression ◽  
Hormone Receptors ◽  
Thyroid Hormone Receptor ◽  
Nuclear Hormone Receptor ◽  
Amino Acid Sequences ◽  
Orphan Receptor ◽  
Primary Amino

Ligand-independent transcriptional repression is an important function of nuclear hormone receptors. An interaction screen with the repression domain of the orphan receptor RevErb identified N-CoR, the corepressor for thyroid hormone receptor (TR) and retinoic acid receptor (RAR). N-CoR is likely to be a bona fide transcriptional corepressor for RevErb because (i) RevErb interacts with endogenous N-CoR, (ii) ectopic N-CoR potentiates RevErb-mediated repression, and (iii) transcriptional repression by RevErb correlates with its ability to bind N-CoR. Remarkably, a region homologous to the CoR box which is necessary for TR and RAR to interact with N-CoR is not required for RevErb. Rather, two short regions of RevErb separated by approximately 200 amino acids are required for interaction with N-CoR. The primary amino acid sequence of the N-terminal region of RevErb essential for N-CoR interaction is not homologous to that of TR or RAR, whereas similarities exist among the C-terminal domains of the receptors. N-CoR contains two adjacent but distinct interaction domains, one of which binds tightly to both RevErb and TR whereas the other binds more weakly and differentially interacts with the nuclear receptors. These results indicate that multiple nuclear receptors, utilizing different primary amino acid sequences, repress transcription by interacting with N-CoR.

Oxytocin amino acid variation within Neotropical primates: new genetic variants in hormone and receptor sequences and evidence for evolutionary forces driving this unexpected diversity

2020 ◽  
Vol 132 (1) ◽  
pp. 211-220
Author(s):  
Susanna K Campbell ◽  
Liliana Cortés-Ortiz
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Specificity ◽  
Selective Constraint ◽  
Neotropical Primates ◽  
Evolutionary Forces ◽  
Amino Acid Variant ◽  
Genes Encoding ◽  
Neuropeptide Hormone ◽  
Amino Acid Sequence Conservation

Abstract Oxytocin is a mammalian neuropeptide hormone that mediates behaviours important to reproduction. Despite almost universal amino acid sequence conservation across most groups of mammals, several unique forms have been reported across Neotropical primates. To explore sequence diversity, we investigated the genes encoding oxytocin and its receptor across the Atelidae, which was known to contain at least three unique oxytocin sequences. Additionally, we included the genus Cebus, within the Cebidae, to further explore the ubiquity of the Pro8 variant in this family. We found a novel amino acid variant (Val3) within the Atelidae radiation, bringing the total number of oxytocin sequences within Neotropical primates to seven. Analyses of physicochemical properties revealed conservative substitutions that are likely tolerated within the selective constraints imposed by receptor binding. Furthermore, we report radical substitutions at the eighth codon and evidence for co-evolution between Pro8 and a ligand-binding region of the oxytocin receptor in the Atelidae, supporting the notion that this variant may affect binding specificity. Overall, we suggest that selective constraint on binding specificity may maintain proper oxytocin function and that the diversification of amino acid sequence is likely due to a variety of processes such as relaxed constraint, neutral mutation, positive selection and coevolution.

scholarly journals The Orphan Nuclear Receptor SHP Inhibits Hepatocyte Nuclear Factor 4 and Retinoid X Receptor Transactivation: Two Mechanisms for Repression

2000 ◽  
Vol 20 (1) ◽  
pp. 187-195 ◽  
Author(s):  
Yoon-Kwang Lee ◽  
Helen Dell ◽  
Dennis H. Dowhan ◽  
Margarita Hadzopoulou-Cladaras ◽  
David D. Moore
Keyword(s):  
Hormone Receptor ◽  
Transcriptional Repressor ◽  
Nuclear Hormone Receptor ◽  
Retinoid X Receptor ◽  
Orphan Receptor ◽  
Receptor Interaction ◽  
Nuclear Factor ◽  
Hepatocyte Nuclear Factor ◽  
Interaction Domain ◽  
Hepatocyte Nuclear Factor 4

ABSTRACT The orphan nuclear hormone receptor SHP interacts with a number of other nuclear hormone receptors and inhibits their transcriptional activity. Several mechanisms have been suggested to account for this inhibition. Here we show that SHP inhibits transactivation by the orphan receptor hepatocyte nuclear factor 4 (HNF-4) and the retinoid X receptor (RXR) by at least two mechanisms. SHP interacts with the same HNF-4 surface recognized by transcriptional coactivators and competes with them for binding in vivo. The minimal SHP sequences previously found to be required for interaction with other receptors are sufficient for interaction with HNF-4, although deletion results indicate that additional C-terminal sequences are necessary for full binding and coactivator competition. These additional sequences include those associated with direct transcriptional repressor activity of SHP. SHP also competes with coactivators for binding to ligand-activated RXR, and based on the ligand-dependent interaction with other nuclear receptors, it is likely that coactivator competition is a general feature of SHP-mediated repression. The minimal receptor interaction domain of SHP is sufficient for full interaction with RXR, as previously described. This domain is also sufficient for full coactivator competition. Functionally, however, full inhibition of RXR transactivation requires the presence of the C-terminal repressor domain, with only weak inhibition associated with this receptor interaction domain. Overall, these results suggest that SHP represses nuclear hormone receptor-mediated transactivation via two separate steps: first by competition with coactivators and then by direct effects of its transcriptional repressor function.

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