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          Institute: MPI für molekulare Genetik     Collection: Ribosome Research Groups     Display Documents

ID: 412557.0, MPI für molekulare Genetik / Ribosome Research Groups
Shine-Dalgarno interaction prevents incorporation of noncognate amino acids at the codon following the AUG
Authors:Di Giacco, Viviana; Márquez, Viter; Yan Qin, Yan; Pech, Markus; Triana-Alonso, Francisco J.; Wilson, Daniel N.; Nierhaus, Knud H.
Date of Publication (YYYY-MM-DD):2008-05-27
Title of Journal:Proceedings of the National Academy of Sciences of the United States of America
Journal Abbrev.:Proc Natl Acad Sci U S A.
Issue / Number:31
Start Page:10715
End Page:10720
Full name of Issue-Editor(s):Edited by Peter B. Moore, Yale University, New Haven, CT,
Copyright:Copyright ©2009 by the National Academy of Sciences
Review Status:not specified
Audience:Experts Only
Abstract / Description:During translation, usually only one in approximately 400 misincorporations affects the function of a nascent protein, because only chemically similar near-cognate amino acids are misincorporated in place of the cognate one. The deleterious misincorporation of a chemically dissimilar noncognate amino acid during the selection process is precluded by the presence of a tRNA at the ribosomal E-site. However, the selection of first aminoacyl-tRNA, directly after initiation, occurs without an occupied E-site, i.e., when only the P-site is filled with the initiator tRNA and thus should be highly error-prone. Here, we show how bacterial ribosomes have solved this accuracy problem: In the absence of a Shine-Dalgarno (SD) sequence, the first decoding step at the A-site after initiation is extremely error-prone, even resulting in the significant incorporation of noncognate amino acids. In contrast, when a SD sequence is present, the incorporation of noncognate amino acids is not observed. This is precisely the effect that the presence of a cognate tRNA at the E-site has during the elongation phase. These findings suggest that during the initiation phase, the SD interaction functionally compensates for the lack of codon-anticodon interaction at the E-site by reducing the misincorporation of near-cognate amino acids and prevents noncognate misincorporation.
External Publication Status:published
Document Type:Article
Communicated by:Ribosome Group
Affiliations:MPI für molekulare Genetik
External Affiliations:1.National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China;
2.Facultad de Ciencias de la Salud, Instituto BIOMED, Universidad de Carabobo, Sede Aragua, Maracay 2101, Venezuela;
3.Gene Center and Department of Chemistry and Biochemistry, Ludwig-Maximilians-Universität, Feodor-Lynen-Strasse 25, D-81377 Munich, Germany.
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