TY - JOUR
T1 - Isolation of two functional retinoid X receptor subtypes from the ixodid tick, Amblyomma americanum (L.)
AU - Guo, Xiaoping
AU - Xu, Qing
AU - Harmon, Margaret A.
AU - Jin, Xiaojing
AU - Laudet, Vincent
AU - Mangelsdorf, David J.
AU - Palmer, Melanie J.
N1 - Funding Information:
The authors would like to thank the Oklahoma State University Recombinant DNA/Protein Resource Facility for the synthesis and purification of synthetic oligonucleotides and for DNA sequencing. We would also like to thank Drs Uli Munderloh and Tim Kurtti for the gift of RNA and protein from ecdysone induced RAE25 cells, Dr Vincent Heinrich for providing a Drosophila melanogaster USP cDNA, and Dr Ron Evans for providing USP antisera. We would like to acknowledge Roberta Kelleher and Angela Scarberry for excellent technical assistance and Drs Jack Dillwith, Daniel Peet, and John Sauer for critical review of the manuscript. This work was supported by Oklahoma Advancement of Science and Technology (OCAST) (HR-16) National Research Initiative Competitive Grants Program (95037302-2360) and Oklahoma Agricultural Experiment Station Hatch (OKL02139) grants to MJP, Howard Hughes Medical Institute (HHMI) and a Robert A. Welch Foundation Grant to DJM, and support from CNRS and the Institut de Lille to VL.
PY - 1998/4/30
Y1 - 1998/4/30
N2 - Retinoid X receptors (RXR) play a central role in a variety of nuclear signaling pathways in both vertebrates and invertebrates. Vertebrate RXRs are encoded by a multigene family whereas the insect RXR homologue, ultraspiracle (USP), is encoded by a single gene. To determine if acarines possess an RXR homologue similar to insect USPs, we isolated cDNAs encoding two distinct RXR genes, AamRXR1 and AamRXR2, from the ixodid tick, Amblyomma americanum (L.). The DNA binding domains share ≃ 95 and 87% identity, respectively, with DNA binding domains from insect USP and vertebrate RXR proteins. However, the ligand binding domains of the AamRXRs are more similar to vertebrate RXRs than to insect USP ligand binding domains ( ~ 71 vs ~ 52%). Northern blot and RT-PCR analysis reveal both unique and overlapping patterns of AamRXR1 and AamRXR2 expression. Transactivation analysis show that bath AamRXRs encode proteins which can form functional ecdysteroid receptors but are unlikely to bind retinoic acids.
AB - Retinoid X receptors (RXR) play a central role in a variety of nuclear signaling pathways in both vertebrates and invertebrates. Vertebrate RXRs are encoded by a multigene family whereas the insect RXR homologue, ultraspiracle (USP), is encoded by a single gene. To determine if acarines possess an RXR homologue similar to insect USPs, we isolated cDNAs encoding two distinct RXR genes, AamRXR1 and AamRXR2, from the ixodid tick, Amblyomma americanum (L.). The DNA binding domains share ≃ 95 and 87% identity, respectively, with DNA binding domains from insect USP and vertebrate RXR proteins. However, the ligand binding domains of the AamRXRs are more similar to vertebrate RXRs than to insect USP ligand binding domains ( ~ 71 vs ~ 52%). Northern blot and RT-PCR analysis reveal both unique and overlapping patterns of AamRXR1 and AamRXR2 expression. Transactivation analysis show that bath AamRXRs encode proteins which can form functional ecdysteroid receptors but are unlikely to bind retinoic acids.
KW - Amblyomma americanum
KW - Ecdysteroid
KW - RXR
KW - Retinoid X receptors
KW - Tick
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U2 - 10.1016/S0303-7207(98)00073-2
DO - 10.1016/S0303-7207(98)00073-2
M3 - Article
C2 - 9705073
AN - SCOPUS:0032580249
SN - 0303-7207
VL - 139
SP - 45
EP - 60
JO - Molecular and Cellular Endocrinology
JF - Molecular and Cellular Endocrinology
IS - 1-2
ER -