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Titolo:
THE EXON STRUCTURE OF THE HUMAN MAGP-2 GENE - SIMILARITY WITH THE MAGP-1 GENE IS CONFINED TO 2 EXONS ENCODING A CYSTEINE-RICH REGION
Autore:
HATZINIKOLAS G; GIBSON MA;
Indirizzi:
UNIV ADELAIDE,DEPT PATHOL ADELAIDE SA 5005 AUSTRALIA UNIV ADELAIDE,DEPT PATHOL ADELAIDE SA 5005 AUSTRALIA
Titolo Testata:
The Journal of biological chemistry
fascicolo: 45, volume: 273, anno: 1998,
pagine: 29309 - 29314
SICI:
0021-9258(1998)273:45<29309:TESOTH>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELASTIN-ASSOCIATED MICROFIBRILS; NF-KAPPA-B; MOLECULAR-CLONING; EXTRACELLULAR MICROFIBRILS; GLYCOPROTEIN-1 MAGP-1; COMPONENT; FIBRILLIN; TRANSCRIPTION; EXPRESSION; TISSUES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
G. Hatzinikolas e M.A. Gibson, "THE EXON STRUCTURE OF THE HUMAN MAGP-2 GENE - SIMILARITY WITH THE MAGP-1 GENE IS CONFINED TO 2 EXONS ENCODING A CYSTEINE-RICH REGION", The Journal of biological chemistry, 273(45), 1998, pp. 29309-29314

Abstract

A cDNA for human microfibril-associated glycoprotein-a (MAGP-2) was used to screen a human leukocyte genomic DNA library in EMBL-3 vector. One clone, clone H (10 kilobase pairs (kbp)), was isolated that contained most of the MAGP-2 gene. The remainder of the 3' end of the gene was obtained by direct polymerase chain reaction amplification of genomic DNA, The human MAGP-2 gene was found to be about 11 kbp in size andto contain 10 evenly distributed exons, The internal exons range in size from 30 base pairs (bp) to 88 bp with exons 4 and 6 the only exonsof equal size (45 bp), All internal intron: exon junctions are defined by canonical splice donor and acceptor sites. Each junction has a 1/2 codon split with the exception of the exon 8/9 junction, which has a2/1 split. The translation initiation codon is in exon 2, and the final exon contains 110 bp of coding sequence, including 2 cysteine codons, Primer extension experiments identified only one major transcription initiation site, 213 bases upstream of the ATG site. Rapid analysis of cDNA ends-polymerase chain reaction analysis of the 5' end of MAGP-2 mRNA from placenta confirmed this result and did not detect any alternative splicing of transcripts,The putative promoter region of the MAGP-2 gene was found to be AT-rich and it lacked a TATA box and other common regulatory elements. However the sequence surrounding the transcription start site CTCA(+1)TTCC was similar to the consensus CTCA(+1)NTCT (N is any nucleoside) for an initiator element found in terminal deoxynucleotidyltransferase and a number of other highly regulated genes. Comparison with the previously characterized human MAGP-1 gene showed that structural similarity was largely confined to the exact size, sequence, and junction alignment of the two penultimate exons which encode the first six of the seven cysteine residues that are precisely spaced in both proteins. The findings are consistent with the growing evidence that, although MAGP-1 and MAGP-2 are both intimately involved in the biology of fibrillin-containing microfibrils, the MAGPs are structurally, functionally, and developmentally diverse proteins which share one characteristic cysteine-rich motif.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 21:37:13