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Originally published In Press as doi:10.1074/jbc.M112395200 on March 7, 2002

J. Biol. Chem., Vol. 277, Issue 21, 18431-18439, May 24, 2002
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Mrd1p Is Required for Processing of Pre-rRNA and for Maintenance of Steady-state Levels of 40 S Ribosomal Subunits in Yeast*

Shao-Bo JinDagger , Jian ZhaoDagger , Petra BjörkDagger , Karin SchmekelDagger , Per. O. Ljungdahl§, and Lars WieslanderDagger

From the Dagger  Department of Molecular Biology and Functional Genomics, Stockholm University, SE-106 91 Stockholm, Sweden and the § Ludwig Institute for Cancer Research, Karolinska Institutet, SE-171 77 Stockholm, Sweden

Ribosome biogenesis is a conserved process in eukaryotes that requires a large number of small nucleolar RNAs and trans-acting proteins. The Saccharomyces cerevisiae MRD1 (multiple RNA-binding domain) gene encodes a novel protein that contains five consensus RNA-binding domains. Mrd1p is essential for viability. Mrd1p partially co-localizes with the nucleolar protein Nop1p. Depletion of Mrd1p leads to a selective reduction of 18 S rRNA and 40 S ribosomal subunits. Mrd1p associates with the 35 S precursor rRNA (pre-rRNA) and U3 small nucleolar RNAs and is necessary for the initial processing at the A0-A2 cleavage sites in pre-rRNA. The presence of five RNA-binding domains in Mrd1p suggests that Mrd1p may function to correctly fold pre-rRNA, a requisite for proper cleavage. Sequence comparisons suggest that Mrd1p homologues exist in all eukaryotes.

* This work was supported by The Swedish Research Council, Natural and Engineering Sciences, Magnus Bergvalls Stiftelse (to L. W.) and Carl Tryggers Stiftelse (to L. W.) and the Ludwig Institute for Cancer Research (to P. O. L.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel: 46-8-161720; Fax: 46-8-166488; E-mail: Lars.Wieslander@molbio.su.se.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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