Structural organization of the gene encoding the human lipocalin tear prealbumin and synthesis of the recombinant protein in Escherichia coli.
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Holzfeind P, Redl B
Structural organization of the gene encoding the human lipocalin tear prealbumin and synthesis of the recombinant protein in Escherichia coli.
Gene. 1994 Feb 25;139(2):177-83.
- PubMed ID
- 8112601 [ View in PubMed]
- Abstract
The genomic DNA fragment encoding the human lipocalin tear prealbumin (LCN1), a new member of the superfamily of hydrophobic molecule transporters, has been isolated and sequenced. The entire gene is approximately 6.2 kb in size and contains six protein-coding exons and a 3'-nontranslated exon. All exon/intron splice junctions exactly follow the GT/AG rule. The structure of the LCN1 gene is highly similar, in terms of numbers and sizes of exons and in intron phasing, to that of the genes encoding ovine beta-lactoglobulin, human placental protein P14, rat alpha 2-urinary globulin, rat prostaglandin D synthase and human alpha 1-microglobulin, thus supporting the close evolutionary relationship of these genes. The 5'-noncoding region of LCN1 contains, besides a TATA and CAAT box, several motifs that resemble regulatory elements of other eukaryotic genes, including potential metal-responsive elements (MRE) and a cAMP-responsive element (CRE). As a basis for further investigations concerning the structure-function relationship and to generate a source of recombinant protein for X-ray crystallography studies, LCN1 was produced in Escherichia coli as a fusion with maltose-binding protein.