Rrb1p, a Yeast Nuclear WD-Repeat Protein Involved in the Regulation of Ribosome Biosynthesis

doi:10.1128/MCB.21.4.1260-1271.2001

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Molecular and Cellular Biology, February 2001, p. 1260-1271, Vol. 21, No. 4
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.4.1260-1271.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Rrb1p, a Yeast Nuclear WD-Repeat Protein Involved in the Regulation of Ribosome Biosynthesis

Tatiana L. Iouk,¹ John D. Aitchison,¹^,² Shawna Maguire,¹ and Richard W. Wozniak¹^,^*

Department of Cell Biology, University of Alberta, Edmonton, Alberta, Canada T6G 2H7,¹ and Institute for Systems Biology, Seattle, Washington 98105-6099²

Received 14 June 2000/Returned for modification 24 July 2000/Accepted 20 November 2000

Ribosome biogenesis is regulated by environmental cues that coordinately modulate the synthesis of ribosomal components andtheir assembly into functional subunits. We have identified anessential yeast WD-repeat-containing protein, termed Rrb1p, thathas a role in both the assembly of the 60S ribosomal subunitsand the transcriptional regulation of ribosomal protein (RP) genes.Rrb1p is located in the nucleus and is concentrated in the nucleolus.Its presence is required to maintain normal cellular levels of60S subunits, 80S ribosomes, and polyribosomes. The function ofRrb1p in ribosome biogenesis appears to be linked to its associationwith the ribosomal protein rpL3. Immunoprecipitation of Rrb1pfrom nuclear extracts revealed that it physically interacts withrpL3. Moreover, the overproduction of Rrb1p led to increases incellular levels of free rpL3 that accumulated in the nucleus togetherwith Rrb1p. The concentration of these proteins within the nucleuswas dependent on ongoing protein translation. We also showed thatoverexpression of RRB1 led to an increase in the expression ofRPL3 while all other examined RP genes were unaffected. In contrast,depletion of RRB1 caused an increase in the expression of allRP genes examined except RPL3. These results suggest that Rrb1pregulates RPL3 expression and uncouples it from the coordinatedexpression of other RPgenes.

^* Corresponding author. Mailing address: 5-14 Medical Sciences Bldg., Department of Cell Biology, University of Alberta, Edmonton,Alberta, Canada T6G 2H7. Phone: (780) 492-1384. Fax: (780) 492-0450.E-mail: rick.wozniak{at}ualberta.ca.

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