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Genomic structure of human lysosomal glycosylasparaginase
Author(s) -
Park Hyejeong,
Fisher Krishna J.,
Aronson Nathan N.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81027-6
Subject(s) - exon , intron , polyadenylation , gene , biology , cpg site , genetics , binding site , untranslated region , microbiology and biotechnology , tata box , promoter , messenger rna , gene expression , dna methylation
The gene structure of the human lysosomal enzyme glycosylasparaginase was determined. The gene spans 13 kb and consists of 9 exons. Both 5′ and 3′ untranslated regions of the gene are uninterrupted by introns. A number of transcriptional elements were identified in the 5′ upstream sequence that includes two putative CAAT boxes followed by TATA‐like sequences together with two AP‐2 binding sites and one for Sp1. A 100 bp CpG island and several ETF binding sites were also found. Additional AP‐2 and Sp1 binding sites are present in the first intron. Two polyadenylation sites are present and appear to be functional. The major known glycosylasparaginase gene defect G 488 →C, which causes the lysosomal storage disease aspartylglycosaminuria (AGU) in Finland, is located in exon 4. Exon 5 encodes the post‐translational cleavage site for the formation of the mature α/β subunits of the enzyme as well as a recently proposed active site threonine, Thr 206 .