Nucleic Acids Research, 1985, Vol. 13, No. 17 6387-6398
© 1985
Articles |
The human apolipoprotein AII gene: structural organization and sites of expression
Molecular Medicine, MRC Clinical Research Centre Harrow, Middlesex, UK +Chiron Corporation 4560 Horton St., Emeryville, CA 94608, USA
Received January 3, 1985. Revised August 2, 1985. Accepted August 9, 1985.
The complete nucleotide sequence of the human apolipoprotein All gene together with 911 bases of 5' flanking sequence and 687 bases of 3' flanking sequence have been determined. The mRNA coding region is interrupted by three introns of 169, 293 and 395bp. The Intron-exon structure of the apo All gene is similar to that of the apo Al, apo CIII and apo E genes: three introns separate 4 coding sequences specifying the 5' untranslated region, pre-peptide, a short N-terminal domain and a C-terminal domain composed of a variable number of lipid-binding amphipathic helices. Intron II carries a 33bp dG-dT repetitive element adjacent to the 3' splice Junction which has the potential to adopt the Z-DNA conformation. The 5' and 3' terminuses of the mRNA have been identified by primer extension and S1 nuclease mapping. A number of short direct repeats are found in the 5' flanking region and an inverted repeat occurs between the CAAT and TATA boxes. Downstream of the the gene is an Alu family repeat containing a polymorphic Mspl site, the deletion of which is associated with increased circulating levels of apoAII. ApoAII gene expression was demonstrated in adult human liver and HepG2 cells but not in human small intestine. Of ten Rhesus monkey tissues examined apo All mRNA was detected only in liver.
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