tailieunhanh - Báo cáo khoa học: Identification and characterization of a nuclear receptor subfamily I member in the Platyhelminth Schistosoma mansoni (SmNR1)

A cDNA encoding a nuclear receptor subfamily I member in the platy-helminthSchistosoma mansoni(SmNR1) was identified and characterized. SmNR1 cDNA is 2406 bp long and contains an open reading frame encoding a 715 residue protein. | ễFEBS Journal Identification and characterization of a nuclear receptor subfamily I member in the Platyhelminth Schistosoma mansoni SmNR1 Wenjie Wu1 Edward G. Niles1 Hirohisa Hirai2 and Philip T. LoVerde1 1 Department of Microbiology and Immunology Schoolof Medicine and BiomedicalScience State University of New York Buffalo NY USA 2 Primate Research Institute Kyoto University Inuyama Japan Keywords nuclear receptors Schistosoma mansoni SmNR1 SmRXR1 interactions Correspondence P. T. LoVerde Southwest Foundation for BiomedicalResearch PO Box 760549 San Antonio TX 78245-0549 USA Fax 1 210 6703322 Tel 1 210 2589852 E-mail ploverde@ Present address Southwest Foundation for Biomedical Research PO Box 760549 San Antonio Texas 78245-0549 USA Note The nucleotide sequences reported in this paper have been submitted to the GenBank under accession number AY395037 AY395051-AY395057 Received 25 September 2006 revised 6 November 2006 accepted 9 November 2006 A cDNA encoding a nuclear receptor subfamily I member in the platy-helminth Schistosoma mansoni SmNR1 was identified and characterized. SmNR1 cDNA is 2406 bp long and contains an open reading frame encoding a 715 residue protein. Phylogenetic analysis demonstrates that SmNR1 is a divergent member of nuclear receptor subfamily I with no known orthologue. SmNRl was localized to S. mansoni chromosome 1 by fluorescent in situ hybridization. Gene structure of SmNRl was determined showing it to consist of eight exons spanning more than 14 kb. Quantitative real-time RT-PCR showed that SmNRl was expressed throughout schistosome development with a higher expression in eggs sporocysts and 21-day worms. SmNR1 contains an autonomous transactivation function AF1 in the A B domain as demonstrated in a yeast one-hybrid assay it interacts with SmRXR1 in a yeast two-hybrid assay and in a glutathione S-transferase pull-down assay. Electrophoretic mobility shift assay showed that SmNR1 could form a heterodimer with SmRXR1 to bind to DNA

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