| Autor: |
Khaĭrulina IuS, Molotkov MV, Bulygin KN, Graĭfer DM, Ven'iaminova AG, Karpova GG |
| Jazyk: |
ruština |
| Zdroj: |
Molekuliarnaia biologiia [Mol Biol (Mosk)] 2008 Mar-Apr; Vol. 42 (2), pp. 306-13. |
| Abstrakt: |
Protein S15 is a characteristic component of the mammalian 80S ribosome that neighbors mRNA codon at the decoding site and the downstream triplets. In this study we determined S15 protein fragments located close to mRNA positions +4 to +12 with respect to the first nucleotide of the P site codon on the human ribosome. For cross-linking to ribosomal protein S15, a set of mRNA was used that contained triplet UUU/UUC at the 5'-termini and a perfluorophenyl azide-modified uridine in position 3' of this triplet. The locations of mRNA analogues on the ribosome were governed by tRNAPhe cognate to the UUU/UUC triplet targeted to the P site. Cross-linked S15 protein was isolated from the irradiated with mild UV light complexes of 80S ribosomes with tRNAPhe and mRNA analogues with subsequent cleavage with CNBr that splits polypeptide chain after methionines. Analysis of modified oligopeptides resulted from the cleavage revealed that in all cases cross-linking site was located in C-terminal fragment 111-145 of protein S15 indicating that this fragment is involved in formation of decoding site of the eukaryotic ribosome. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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