PIN domain of Nob1p is required for D-site cleavage in 20S pre-rRNA

RNA
Alessandro FaticaMensur Dlakić

Abstract

Nob1p (Yor056c) is essential for processing of the 20S pre-rRNA to the mature 18S rRNA. It is part of a pre-40S ribosomal particle that is transported to the cytoplasm and subsequently cleaved at the 3' end of mature 18S rRNA (D-site). Nob1p is also reported to participate in proteasome biogenesis, and it was therefore unclear whether its primary activity is in ribosome synthesis. In this work, we describe a homology model of the PIN domain of Nob1p, which structurally mimics Mg(2+)-dependent exonucleases despite negligible similarity in primary sequence. Insights gained from this model were used to design a point mutation that was predicted to abolish the postulated enzymatic activity. Cells expressing Nob1p with this mutation failed to cleave the 20S pre-rRNA. This supports both the significance of the structural model and the idea that Nob1p is the long-sought D-site endonuclease.

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Citations

Jun 14, 2006·Proceedings of the National Academy of Sciences of the United States of America·Franziska BleichertSusan J Baserga
Oct 9, 2014·Nucleic Acids Research·Tomasz W TurowskiDavid Tollervey
Sep 9, 2005·Nucleic Acids Research·Anton V Borovjagin, Susan A Gerbi
Oct 7, 2005·Genome Biology·Mensur Dlakić
Nov 17, 2005·Molecular and Cellular Biology·Sander GrannemanSusan J Baserga
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Dec 9, 2008·Nature Structural & Molecular Biology·Daneen SchaefferAmbro van Hoof
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Jan 27, 2010·Nucleic Acids Research·Juliane MerlHerbert Tschochner
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Dec 14, 2011·Nucleic Acids Research·Thomas VeithEnrico Schleiff
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