MersV1, France, Analysis, bibRecord, 000276

Isolation of a functional ecdysteroid receptor homologue from the ixodid tick Amblyomma americanum (L.)

Identifieur interne : 000276 ( France/Analysis ); précédent : 000275; suivant : 000277

Isolation of a functional ecdysteroid receptor homologue from the ixodid tick Amblyomma americanum (L.)

Auteurs : Xiaoping Guo [États-Unis] ; Margaret A. Harmon [États-Unis] ; Vincent Laudet [France] ; David J. Mangelsdorf [États-Unis] ; Melanie J. Palmer [États-Unis]

Source :

Insect Biochemistry and Molecular Biology [ 0965-1748 ] ; 1997.

RBID : ISTEX:98E65344AFE5B84E505070DD9E8ED920B10A9400

English descriptors

Teeft :
- Aamecr, Aamecr clusters, Aamecr gene, Aamecr gene encodes, Aamecr isoform, Aamecr mrnas, Aamecr sequence, Aamecr transcripts, Aamecra1, Aamecra2, Aamecra3, Aamecra3 mrna, Aamecra3 transcripts, Aamrxr, Amblyomma, Amblyomma americanum, Americanum, Amino, Amino acid sequence, Amino acids, Arthropod, Assay, Behavioral biology, Biochemistry, Bottom panel, Cdna, Cdna libraries, Cherbas, Common region, Complex processing, Conservative changes, Diehl, Distance analysis, Drosophila, Ecdysone, Ecdysone receptor, Ecdysteroid, Ecdysteroid receptor, Ecdysteroids, Ecre, Ecrs, Embryo, Encodes, Encoding, Functional ecdysone receptor, Functional ecdysteroid receptor, Gene, Heterogeneous populations, High degree, Homologue, Insect biochemistry, Insect counterparts, Insect ecrs, Isoform, Isoforms, Ixodid, Ixodid ticks, John wiley, Kaufman, Larva, Larval, Life cycle, Ligand, Ligand binding, Linker primer, Mangelsdorf, Methylmercuric hydroxide, Molecular biology, Molecular weight, Mrna, Mrna expression, Multiple cdnas, National academy, Northern blot analysis, Nuclear receptor superfamily, Nucleic acids research, Nucleotide, Nucleotide position, Nymph, Orfs, Other arthropods, Parsimony analysis, Phylogenetic analysis, Plasmid, Primer, Promoter, Putative, Receptor, Retinoic acid, Right panel, Salivary, Salivary gland, Salivary glands, Sauer, Several cdnas, Smaller bands, Sonnenshine, Southern blot analysis, Substitution, Superfamily, Talbot, Terminus, Tick, Tmecr, Topology, Transcript, Vertebrate, Xiaoping.

Abstract

Abstract: Ecdysteroids are assumed to be the major steroid hormones in arthropods. However, with the exception of insects and crustaceans, very little is known about ecdysteroid action in other arthropods. To determine if ecdysteriods play a functional role in the ixodid tick, Amblyomma americanum (L.), we isolated cDNAs encoding three presumed ecdysteroid receptor isoforms (AamEcRA1, AamEcRA2, and AamEcRA3) that have common DNA and ligand binding domains linked to distinct amino termini. The DNA and ligand binding domains share an average of 86 and 64% identity, respectively with DNA and ligand binding domains from insect EcR proteins. The amino termini are highly divergent and the AamEcRs lack the `F' domain found in the insect EcRs. Analysis of AamEcR cDNAs show that processing of the AamEcR gene is complex, producing multiple transcripts with unique 5′ and 3′ termini as well as splicing variants with incomplete open reading frames. AamEcR mRNA profiles in whole animals and isolated tissues are consistent with complex regulation of AamEcR expression. We also examined the ability of AamEcRA1, when paired with an AamRXR, to activate transcription of an ecdysone response element containing reporter, and demonstrate that the AamEcR gene encodes a functional ecdysteroid receptor.

Url:

https://api.istex.fr/ark:/67375/6H6-GDTXL577-Z/fulltext.pdf

DOI: 10.1016/S0965-1748(97)00075-1

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Istex, to step Corpus: 002574
to stream Istex, to step Curation: 002574
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to stream Main, to step Curation: 003A58
to stream Main, to step Exploration: 003A58
to stream France, to step Extraction: 000276

Links to Exploration step

ISTEX:98E65344AFE5B84E505070DD9E8ED920B10A9400

Le document en format XML

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<front><div type="abstract" xml:lang="en">Abstract: Ecdysteroids are assumed to be the major steroid hormones in arthropods. However, with the exception of insects and crustaceans, very little is known about ecdysteroid action in other arthropods. To determine if ecdysteriods play a functional role in the ixodid tick, Amblyomma americanum (L.), we isolated cDNAs encoding three presumed ecdysteroid receptor isoforms (AamEcRA1, AamEcRA2, and AamEcRA3) that have common DNA and ligand binding domains linked to distinct amino termini. The DNA and ligand binding domains share an average of 86 and 64% identity, respectively with DNA and ligand binding domains from insect EcR proteins. The amino termini are highly divergent and the AamEcRs lack the `F' domain found in the insect EcRs. Analysis of AamEcR cDNAs show that processing of the AamEcR gene is complex, producing multiple transcripts with unique 5′ and 3′ termini as well as splicing variants with incomplete open reading frames. AamEcR mRNA profiles in whole animals and isolated tissues are consistent with complex regulation of AamEcR expression. We also examined the ability of AamEcRA1, when paired with an AamRXR, to activate transcription of an ecdysone response element containing reporter, and demonstrate that the AamEcR gene encodes a functional ecdysteroid receptor.</div>
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   |texte=   Isolation of a functional ecdysteroid receptor homologue from the ixodid tick Amblyomma americanum (L.)
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Isolation of a functional ecdysteroid receptor homologue from the ixodid tick Amblyomma americanum (L.)

Isolation of a functional ecdysteroid receptor homologue from the ixodid tick Amblyomma americanum (L.)

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

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