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J. Biol. Chem., Vol. 278, Issue 9, 6635-6641, February 28, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/9/6635    most recent M212220200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lee, Y. Articles by Nazar, R. N. Search for Related Content PubMed PubMed Citation Articles by Lee, Y. Articles by Nazar, R. N. Social Bookmarking                      What's this?

Terminal Structure Mediates 5 S rRNA Stability and Integration during Ribosome Biogenesis^*

Yoon Lee and Ross N. Nazar

From the Department of Molecular Biology and Genetics, University of Guelph, Guelph, Ontario N1G 2W1, Canada

Formation of the eukaryotic ribosomal 5 S RNA-protein complex has been shown to be critical to ribosome biogenesis and has been speculated to contribute to a quality control mechanism that helps ensure that only normal precursors are processed and assembled into active ribosomes. To study the structural basis of these observations, the RNA-protein interface in the 5 S RNA-protein complex of the yeast (Saccharomyces cerevisiae) ribosome was examined based on a systematic introduction of targeted base substitutions in the RNA sequence. Most base substitutions had little or no effect on the efficiency of complex formation, but large effects were observed when changes disrupted helix I, the secondary structure formed between the interacting termini. Again, only modest effects were evident when the extended 3' end of the mature RNA molecule was altered, but essentially no complex was formed when the 5' end of the mature 5 S RNA sequence was artificially extended by one nucleotide. In vitro analyses demonstrated that this extension also dramatically altered the maturation of 5 S rRNA precursor molecules as well as the stability of the mature 5 S rRNA. Taken together, the results indicate that in the course of RNA maturation, the 5 S RNA-binding protein binds precisely over or "caps" the termini in a critical manner that protects the RNA from further degradation.

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