| First Author | Waris T | Year | 1992 |
| Journal | Biochem Biophys Res Commun | Volume | 189 |
| Issue | 1 | Pages | 424-9 |
| PubMed ID | 1449493 | Mgi Jnum | J:3337 |
| Mgi Id | MGI:51850 | Doi | 10.1016/0006-291x(92)91575-b |
| Citation | Waris T, et al. (1992) Molecular cloning of the mouse S-adenosylmethionine decarboxylase cDNA: specific protein binding to the conserved region of the mRNA 5'-untranslated region. Biochem Biophys Res Commun 189(1):424-9 |
| abstractText | The nucleotide sequence of a cDNA encoding the proenzyme of mouse S-adenosylmethionine decarboxylase (AdoMetDC) including 257 nucleotides of the 5' untranslated region has been determined. Comparison of the nucleotide sequence of the mouse 5' untranslated region with those of other mammals shows it to be highly conserved. The 52 nucleotides upstream from the translation initiation codon are identical in human, rat, bovine and mouse. The polyamines, spermidine and spermine, have been shown to inhibit AdoMetDC mRNA translation. An RNA gel retardation assay demonstrated that a cytoplasmic extract from mouse brain forms an RNA-protein complex with the completely conserved 5' untranslated sequence and that the complex formation is highly dependent on the presence of spermine. Crosslinking by UV irradiation shows that the complex contains a 39-kDa protein interacting with the 5' untranslated sequence. These data demonstrate spermine-dependent specific protein binding to a highly conserved 5' untranslated region of an mRNA translationally regulated by polyamines. |
