Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-3-25
pubmed:databankReference
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
139
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
177-83
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Structural organization of the gene encoding the human lipocalin tear prealbumin and synthesis of the recombinant protein in Escherichia coli.
pubmed:affiliation
Institut für Mikrobiologie (Med. Fak.), Universität Innsbruck, Austria.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't