Molecular cloning and analysis of functional cDNA and genomic clones encoding bovine cellular retinoic acid-binding protein

Shubeita, H.E.; Sambrook, J.F.; McCormick, A.M.

Proceedings of the National Academy of Sciences of the United States of America 84(16): 5645-5649


ISSN/ISBN: 0027-8424
PMID: 3039499
DOI: 10.2307/30096
Accession: 001638101

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A recombinant cDNA clone, pCRABP-HS1, encoding cellular retinoic acid-binding protein was isolated from a bovine adrenal cDNA library. COS-7 cells transfected with pCRABP-HS1 produced a biologically active retinoic acid-binding protein molecule of the expected molecular mass (15.5 kDa). RNA blot hybridization analysis using pCRABP-HS1 as a probe revealed a single 1050-nucleotide mRNA species in bovine adrenal, uterus, and testis, tissues that contain the highest levels of retinoic acid-binding activity. No hybridization was detected in RNA extracted from ovary, spleen, kidney, or liver, which contain relatively low levels of cellular retinoic acid-binding protein activity. Analysis of genomic clones isolated from an EcoRI bovine genomic library demonstrated that the bovine cellular retinoic acid-binding protein gene is composed of four exons and three introns. Two putative promoter sequences were identified in the cloned 5' sequence of the gene.