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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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Volume 381, Issue 2


Effects of the Active Aldehyde Group Generated by RNA N-Glycosidase in the Sarcin/Ricin Domain of Rat 28S Ribosomal RNA on Peptide Elongation

Yong-Zhen Xu / Wang-Yi Liu
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2000.016


Effects of the active aldehyde group of ribose C′1 at position 4324 of rat 28S rRNA, in the inactivated ribosome generated by RNA N-glycosidases (trichosanthin, A-chain of cinnamomin and ricin), on peptide elongation have been studied. The aldehyde group inhibits the activities of eEF1A-dependent aminoacyltRNA binding to the inactivated ribosome and eEF1Adependent GTPase, but increases eEF2-dependent activity. At a high concentration of RNA N-glycosidase, the generated aldehyde group also inhibits aminoacyl-tRNA binding to the inactivated ribosome in the absence of elongation factor and translocation activity. When the aldehyde group is reduced into a hydroxyl group by sodium borohydride or blocked with an amino acid through nucleophilic addition, the activities of eEF1A-dependent aminoacyl-tRNA binding and eEF1A-dependent GTPase of the inactivated ribosome are partially restored, but the altered activities of eEF2-dependent GTPase, translocation and aminoacyl-tRNA binding in the absence of elongation factor are not normalized. Thus, reduction or blockage of the aldehyde group with sodium borohydride or amino acids might change the conformation of the S/R domain in rat 28S ribosomal RNA to meet the requirement for eEF1A-dependent reactions, but not eEF2-involved reactions.

About the article

Published Online: 2005-06-01

Published in Print: 2000-02-15

Citation Information: Biological Chemistry, Volume 381, Issue 2, Pages 113–119, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2000.016.

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