Mrd1p is required for processing of pre-rRNA and for maintenance of steady-state levels of 40S ribosomal subunits in yeast

doi:10.1074/jbc.M112395200

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Papers In Press, published online ahead of print March 7, 2002
J. Biol. Chem, 10.1074/jbc.M112395200
Submitted on December 27, 2001
Revised on March 6, 2002
Accepted on March 7, 2002

Mrd1p is required for processing of pre-rRNA and for maintenance of steady-state levels of 40S ribosomal subunits in yeast

Shao-Bo Jin, Jian Zhao, Petra Björk, Karin Schmekel, Per O. Ljungdahl, and Lars Wieslander

Dept. of Molecular Biology and Functional genomics, Stockholm university, Stockholm SE-106 91

Corresponding Author: Lars.Wieslander{at}molbio.su.se

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 18S rRNA and 40S ribosomal subunits. Mrd1p associates with the 35S pre-rRNA and U3 snoRNA 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.

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