Structure of the human zinc finger protein HIVEP3: Molecular cloning, expression, exon-intron structure, and comparison with paralogous genes HIVEP1 and HIVEP2

被引:28
作者
Hicar, MD
Liu, YL
Allen, CE
Wu, LC
机构
[1] Ohio State Univ, Coll Med & Publ Hlth, Dept Internal Med, Davis Med Ctr,Div Immunol, Columbus, OH 43210 USA
[2] Ohio State Univ, Coll Med & Publ Hlth, Dept Mol Virol Immunol & Med Genet, Columbus, OH 43210 USA
[3] Ohio State Univ, Coll Med & Publ Hlth, Dept Mol & Cellular Biochem, Columbus, OH 43210 USA
[4] Ohio State Univ, Coll Med & Publ Hlth, Mol Cellular & Dev Biol Program, Columbus, OH 43210 USA
关键词
D O I
10.1006/geno.2000.6425
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Here we report the cloning and characterization of HITEP3; the newest member in the human immunodeficiency virus type 1 enhancer-binding protein family that encodes large zinc finger proteins and regulates transcription via the KB enhancer motif. The largest open reading frame of HIVEP3 contains 2406 aa. and is similar to 80% identical to the mouse counterpart. The HIVEP3 gene is located in the chromosomal region 1p34 and is at least 300 kb with 10 exons. RNA studies show that multiple HP3 transcripts are differentially expressed and regulated. Additionally, transcription termination occurs in the ultimate exon, exon 10, or in exon 6. Therefore, HIVEP3 may produce protein isoforms that contain or exclude the carboxyl DNA binding domain and the leucine zipper by alternative RNA splicing and differential polyadenylation. Sequence homologous to HIVEP3 exon 6 is not found in mouse nor are the paralogous genes HIVEP1 and HIVEP2. Zoo-blot analysis suggests that sequences homologous to the human exon 6 are present only in primates and cow. Therefore, a foreign DNA harboring a termination exon likely was inserted into the HIVEP3 locus relatively recently in evolution, resulting in the acquisition of novel gene regulatory mechanisms as well as the generation of structural and functional diversity. (C) 2001 Academic Press.
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页码:89 / 100
页数:12
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