INHIBITION OF RIBOSOMAL-SUBUNIT ASSOCIATION AND PROTEIN-SYNTHESIS BY OLIGONUCLEOTIDES CORRESPONDING TO DEFINED REGIONS OF 18S RIBOSOMAL-RNAAND 5S RIBOSOMAL-RNA

Citation
Aa. Azad et al., INHIBITION OF RIBOSOMAL-SUBUNIT ASSOCIATION AND PROTEIN-SYNTHESIS BY OLIGONUCLEOTIDES CORRESPONDING TO DEFINED REGIONS OF 18S RIBOSOMAL-RNAAND 5S RIBOSOMAL-RNA, Biochemical and biophysical research communications (Print), 248(1), 1998, pp. 51-56
Citations number
40
Categorie Soggetti
Biology,Biophysics
ISSN journal
0006291X
Volume
248
Issue
1
Year of publication
1998
Pages
51 - 56
Database
ISI
SICI code
0006-291X(1998)248:1<51:IORAAP>2.0.ZU;2-G
Abstract
Strong complementarity between a conserved sequence near the 3' end of 18S (16S) rRNA of the small ribosomal subunit and a conserved sequenc e in the 5S rRNA of the large ribosomal subunit supported the suggesti on that base-paired interaction between the two RNA molecules could be responsible for the reversible association of ribosomal subunits duri ng protein synthesis. If this were true then oligonucleotides correspo nding to defined regions of the 18S and 5S rRNAs should have profound effects on the association of ribosomal subunits and protein synthesis . In this report we show that oligonucleotides, corresponding to a def ined region of eukaryotic 18S rRNA, when bound to wheat embryo 60S rib osomal subunits, inhibited association with 40S ribosomal subunits and also inhibited in vitro protein synthesis. Similarly oligonucleotides corresponding to a defined region of 5S rRNA when bound to 40S riboso mal subunits also inhibited the formation of 80S ribosomes and in vitr o protein synthesis. The minimum sequences responsible for the inhibit ion of ribosomal subunit association and in. vitro protein synthesis c orresponded to the 5' strand of the m(2)(6)A m(2)(6)A hairpin structur e near the 3' end of 18S rRNA and nucleotides 91-100 of 5S rRNA which are complementary to each other. Sequences at identical positions of E scherichia coil 16S and 5S rRNAs are also complementary to each other. (C) 1998 Academic Press.