DR-78, A NOVEL DROSOPHILA-MELANOGASTER GENOMIC DNA FRAGMENT HIGHLY HOMOLOGOUS TO THE DNA-BINDING DOMAIN OF THYROID-HORMONE RETINOIC ACID VITAMIN-D RECEPTOR SUBFAMILY
E. Martinblanco et Tb. Kornberg, DR-78, A NOVEL DROSOPHILA-MELANOGASTER GENOMIC DNA FRAGMENT HIGHLY HOMOLOGOUS TO THE DNA-BINDING DOMAIN OF THYROID-HORMONE RETINOIC ACID VITAMIN-D RECEPTOR SUBFAMILY, Biochimica et biophysica acta, 1216(2), 1993, pp. 339-341
Degenerate oligodeoxyribonucleotides were designed for both ends of th
e DNA-binding domain of members of the nuclear receptor superfamily. P
CR amplified Drosophila melanogaster DNA was purified and cloned (DR p
lasmids). Genomic lambdaDASH clones were identified at high stringency
with an amplified DR-78 plasmid DNA and isolated. The partial sequenc
e shows a very probable open reading frame which would encode a peptid
e highly homologous to members of the thyroid hormone-retinoic acid-vi
tamin D receptor subfamily. The fragment corresponds to a single copy
gene and was mapped at position 78D of chromosome three by in situ hyb
ridization.