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Nucleic Acids Research 2005 33(2):478-485; doi:10.1093/nar/gki194
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Published online 19 January 2005

© 2005, the authors Nucleic Acids Research, Vol. 33 No. 2 © Oxford University Press 2005; all rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use permissions, please contact journals.permissions{at}oupjournals.org.

Article

Ribosomal protein L1 recognizes the same specific structural motif in its target sites on the autoregulatory mRNA and 23S rRNA

Natalia Nevskaya, Svetlana Tishchenko, Azat Gabdoulkhakov, Ekaterina Nikonova, Oleg Nikonov, Alexei Nikulin, Olga Platonova1, Maria Garber, Stanislav Nikonov and Wolfgang Piendl1,*

Institute of Protein Research, Russian Academy of Sciences 142290 Pushchino, Moscow region, Russia 1 Innsbruck Medical University, Biocentre Fritz-Prengl-Str.3, A-6020 Innsbruck, Austria

*To whom correspondence should be addressed: Tel: +43 512 507 3531; Fax: +43 512 507 2872; Email: Wolfgang.Piendl{at}uibk.ac.at

Received November 23, 2004. Revised December 24, 2004. Accepted December 24, 2004.

The RNA-binding ability of ribosomal protein L1 is of profound interest since the protein has a dual function as a ribosomal protein binding rRNA and as a translational repressor binding its mRNA. Here, we report the crystal structure of ribosomal protein L1 in complex with a specific fragment of its mRNA and compare it with the structure of L1 in complex with a specific fragment of 23S rRNA determined earlier. In both complexes, a strongly conserved RNA structural motif is involved in L1 binding through a conserved network of RNA–protein H-bonds inaccessible to the solvent. These interactions should be responsible for specific recognition between the protein and RNA. A large number of additional non-conserved RNA–protein H-bonds stabilizes both complexes. The added contribution of these non-conserved H-bonds makes the ribosomal complex much more stable than the regulatory one.

DDBJ/EMBL/GenBank accession no. 1U63


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