Abstract
The UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase catalyzes the first and committed step in the dolichol cycle, thus playing a fundamental role in the pathway for protein N -glycosylation. The structure of the GlcNAc-1-P transferase gene has been previously elucidated in mouse and hamster. Moreover, the human cDNA has been cloned. Using sequence database tools, we deduced the genomic structure of the human GlcNAc-1-P transferase gene, which was experimentally confirmed by sequence analysis. The gene is composed of 9 exons and spans 5.5 kb. All splice acceptor and donor sites conform to the canonical AG/GT rule. The 5′-end of the gene is different from previously reported, as, consequently, the N-terminal of the encoded protein, which is predicted to be 408 amino acids long. The transcription start site, determined by 5′ RACE, occurs 180 nucleotides upstream of the translation initiation codon. Several potential transcription regulatory motifs, such as Sp-1, E4TF1 and ATF binding sites, were identified in the 5′-flanking region. A polyadenylation signal is located 466 bp downstream of the stop codon. The genomic organization of the gene is similar to that of the corresponding mouse and hamster genes, though extensive homology is restricted to the coding regions. Analysis of a panel of radiation hybrids led to the assignment of the GlcNAc-1-P transferase gene to chromosome 11, at 4.19 cR from NIB361, according to the location of the homologous sequences in the database at 11q23.
| Original language | English |
|---|---|
| Pages (from-to) | 245-250 |
| Number of pages | 6 |
| Journal | Mitochondrial DNA |
| Volume | 13 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 2002 |
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Keywords
- Dolichol cycle
- Genome
- GlcNAc-1-P transferase gene
- Glycosyltransferase
ASJC Scopus subject areas
- Genetics
- Molecular Biology
- Biochemistry
- Endocrinology
Cite this
Genomic structure of the human UDP-GlcNAc : dolichol-P GlcNAc-1-P transferase gene. / Regis, Stefano; Dagnino, Fabio; Caroli, Francesco; Filocamo, Mirella.
In: Mitochondrial DNA, Vol. 13, No. 5, 2002, p. 245-250.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Genomic structure of the human UDP-GlcNAc
T2 - dolichol-P GlcNAc-1-P transferase gene
AU - Regis, Stefano
AU - Dagnino, Fabio
AU - Caroli, Francesco
AU - Filocamo, Mirella
PY - 2002
Y1 - 2002
N2 - The UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase catalyzes the first and committed step in the dolichol cycle, thus playing a fundamental role in the pathway for protein N -glycosylation. The structure of the GlcNAc-1-P transferase gene has been previously elucidated in mouse and hamster. Moreover, the human cDNA has been cloned. Using sequence database tools, we deduced the genomic structure of the human GlcNAc-1-P transferase gene, which was experimentally confirmed by sequence analysis. The gene is composed of 9 exons and spans 5.5 kb. All splice acceptor and donor sites conform to the canonical AG/GT rule. The 5′-end of the gene is different from previously reported, as, consequently, the N-terminal of the encoded protein, which is predicted to be 408 amino acids long. The transcription start site, determined by 5′ RACE, occurs 180 nucleotides upstream of the translation initiation codon. Several potential transcription regulatory motifs, such as Sp-1, E4TF1 and ATF binding sites, were identified in the 5′-flanking region. A polyadenylation signal is located 466 bp downstream of the stop codon. The genomic organization of the gene is similar to that of the corresponding mouse and hamster genes, though extensive homology is restricted to the coding regions. Analysis of a panel of radiation hybrids led to the assignment of the GlcNAc-1-P transferase gene to chromosome 11, at 4.19 cR from NIB361, according to the location of the homologous sequences in the database at 11q23.
AB - The UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase catalyzes the first and committed step in the dolichol cycle, thus playing a fundamental role in the pathway for protein N -glycosylation. The structure of the GlcNAc-1-P transferase gene has been previously elucidated in mouse and hamster. Moreover, the human cDNA has been cloned. Using sequence database tools, we deduced the genomic structure of the human GlcNAc-1-P transferase gene, which was experimentally confirmed by sequence analysis. The gene is composed of 9 exons and spans 5.5 kb. All splice acceptor and donor sites conform to the canonical AG/GT rule. The 5′-end of the gene is different from previously reported, as, consequently, the N-terminal of the encoded protein, which is predicted to be 408 amino acids long. The transcription start site, determined by 5′ RACE, occurs 180 nucleotides upstream of the translation initiation codon. Several potential transcription regulatory motifs, such as Sp-1, E4TF1 and ATF binding sites, were identified in the 5′-flanking region. A polyadenylation signal is located 466 bp downstream of the stop codon. The genomic organization of the gene is similar to that of the corresponding mouse and hamster genes, though extensive homology is restricted to the coding regions. Analysis of a panel of radiation hybrids led to the assignment of the GlcNAc-1-P transferase gene to chromosome 11, at 4.19 cR from NIB361, according to the location of the homologous sequences in the database at 11q23.
KW - Dolichol cycle
KW - Genome
KW - GlcNAc-1-P transferase gene
KW - Glycosyltransferase
UR - http://www.scopus.com/inward/record.url?scp=0036806517&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036806517&partnerID=8YFLogxK
U2 - 10.1080/1042517021000017126
DO - 10.1080/1042517021000017126
M3 - Article
VL - 13
SP - 245
EP - 250
JO - DNA Sequence - Journal of DNA Sequencing and Mapping
JF - DNA Sequence - Journal of DNA Sequencing and Mapping
SN - 1940-1736
IS - 5
ER -