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Molecular and Cellular Biology, July 2004, p. 6476-6487, Vol. 24, No. 14
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.14.6476-6487.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Diazaborine Treatment of Yeast Cells Inhibits Maturation of the 60S Ribosomal Subunit

Brigitte Pertschy, Gertrude Zisser, Hermine Schein, René Köffel,{dagger} Gernot Rauch, Karlheinz Grillitsch, Christina Morgenstern, Michael Durchschlag, Gregor Högenauer,* and Helmut Bergler

Institut für Molekularbiologie, Biochemie und Mikrobiologie, Karl-Franzens-Universität Graz, A-8010 Graz, Austria

Received 2 February 2004/ Returned for modification 8 March 2004/ Accepted 19 April 2004

Diazaborine treatment of yeast cells was shown previously to cause accumulation of aberrant, 3'-elongated mRNAs. Here we demonstrate that the drug inhibits maturation of rRNAs for the large ribosomal subunit. Pulse-chase analyses showed that the processing of the 27S pre-rRNA to consecutive species was blocked in the drug-treated wild-type strain. The steady-state level of the 7S pre-rRNA was clearly reduced after short-term treatment with the inhibitor. At the same time an increase of the 35S pre-rRNA was observed. Longer incubation with the inhibitor resulted in a decrease of the 27S precursor. Primer extension assays showed that an early step in 27S pre-rRNA processing is inhibited, which results in an accumulation of the 27SA2 pre-rRNA and a strong decrease of the 27SA3, 27SB1L, and 27SB1S precursors. The rRNA processing pattern observed after diazaborine treatment resembles that reported after depletion of the RNA binding protein Nop4p/Nop77p. This protein is essential for correct pre-27S rRNA processing. Using a green fluorescent protein-Nop4 fusion, we found that diazaborine treatment causes, within minutes, a rapid redistribution of the protein from the nucleolus to the periphery of the nucleus, which provides a possible explanation for the effect of diazaborine on rRNA processing.

* Corresponding author. Mailing address: Institut für Molekularbiologie, Biochemie und Mikrobiologie, Karl-Franzens-Universität Graz, Universitätsplatz 2, A-8010 Graz, Austria. Phone: 43-316-380-5683. Fax: 43-316-380-9898. E-mail: gregor.hoegenauer{at}uni-graz.at.

{dagger} Present address: Department of Medicine, Division of Biochemistry, University of Fribourg, CH-1700 Fribourg, Switzerland.

Molecular and Cellular Biology, July 2004, p. 6476-6487, Vol. 24, No. 14
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.14.6476-6487.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Pertschy, B., Saveanu, C., Zisser, G., Lebreton, A., Tengg, M., Jacquier, A., Liebminger, E., Nobis, B., Kappel, L., van der Klei, I., Hogenauer, G., Fromont-Racine, M., Bergler, H. (2007). Cytoplasmic Recycling of 60S Preribosomal Factors Depends on the AAA Protein Drg1. Mol. Cell. Biol. 27: 6581-6592 [Abstract] [Full Text]  


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