Nucleic Acids Research Advance Access originally published online on February 7, 2007
Nucleic Acids Research 2007 35(5):1514-1521; doi:10.1093/nar/gkl1121
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Nucleic Acids Research, 2007, Vol. 35, No. 5 1514-1521
© 2007 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Eukaryotic ribosomal protein RPS25 interacts with the conserved loop region in a dicistroviral intergenic internal ribosome entry site
1National Institute of Agrobiological Sciences, Owashi, Tsukuba, Ibaraki, 305-8634, Japan and 3Faculty of Science, Niigata University, Igarasi 2-8050, Niigata, 950-2181, Japan
*To whom correspondence should be addressed. Tel: +81-29-838-6166; Fax: +81-29-838-6028; Email: nakaji{at}affrc.go.jp
Received September 6, 2006. Revised December 10, 2006. Accepted December 10, 2006.
The intergenic region-internal ribosome entry site (IGR-IRES) of dicistroviruses binds to 40S ribosomal subunits in the absence of eukaryotic initiation factors (eIFs). Although the conserved loop sequences in dicistroviral IGR-IRES elements are protected from chemical modifications in the presence of the 40S subunit, molecular components in the 40S subunit, which interacts with the loop sequences in the IRES, have not been identified. Here, a chemical crosslinking study using 4-thiouridine-labeled IGR-IRES revealed interactions of the IGR-IRES with several 40S proteins but not with the 18S rRNA. The strongest crosslinking signal was identified for ribosomal protein S25 (rpS25). rpS25 is known to be a neighbor of rpS5, which has been shown to interact with a related IGR-IRES by cryo-electron microscopy. Crosslinking analysis with site-directed mutants showed that nucleotides UU6089–6090, which are located in the loop region in conserved domain 2b in the IRES, appear to interact with rpS25. rpS25 is specific to eukaryotes, which explains why there is no recognition of the IGR-IRES by prokaryotic ribosomes. Although the idea that the IGR-IRES element may be a relict of a primitive translation system has been postulated, our experimental data suggest that the IRES has adapted to eukaryotic ribosomal proteins.
2Present address: Faculty of Biotechnology and Life Science, Sojo University, Kumamoto, 860-0082, Japan
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