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Conformational changes of L-rRNA during elongation of polypeptide.

Abstract：

:A ribosome undergoes significant conformational changes during elongation of a polypeptide chain, and these are correlated with structural changes of rRNAs. We tested 15 different oligonucleotides complementary to the selected, highly conserved seqences of rRNAs (L-rRNA, 5S rRNA and tRNA) important in protein biosynthesis. We carried out a reaction of binding Phe-tRNA to A site and a polymerization of polypeptide chains on the ribosomes converted either to pre- or to posttranslocational states. The inhibition of polymerization reaction by complementary oligonucleotides was high in all ribosomal states. The efficiency of inhibition of binding reaction was lower and more diverse than was the polypeptide elongation. We conclude that the selected oligonucleotides inhibit polypeptide synthesis with different effectivity, primarily depending on L-rRNA conformation within ribosome architecture.

journal_name

J Plant Physiol

journal_title

Journal of plant physiology

authors

Dudzińska-Bajorek B,Bakowska K,Twardowski T

doi

10.1016/j.jplph.2005.03.016

subject

Has Abstract

pub_date

2006-03-01 00:00:00

pages

463-74

issue

4

eissn

0176-1617

issn

1618-1328

pii

S0176-1617(05)00179-3

journal_volume

163

pub_type

杂志文章

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