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Nucleic Acids Research, 2003, Vol. 31, No. 23 6798-6805
© 2003 Oxford University Press

Article

Ribosomal proteins Rps0 and Rps21 of Saccharomyces cerevisiae have overlapping functions in the maturation of the 3' end of 18S rRNA

Amy Tabb-Massey1, Jacqueline M. Caffrey1, Paula Logsden1, Stephen Taylor1, John O. Trent1,2,3 and Steven R. Ellis*,1,3

1 Department of Biochemistry and Molecular Biology and 2 Department of Medicine, University of Louisville, Louisville, KY 40292, USA and 3 The James Graham Brown Cancer Center, Louisville, KY, USA

*To whom correspondence should be addressed. Tel: +1 502 852 5222; Fax: +1 502 852 6222; Email: srellis{at}louisville.edu

The Rps0 proteins of Saccharomyces cerevisiae are components of the 40S ribosomal subunit required for maturation of the 3' end of 18S rRNA. Drosophila and human homologs of the Rps0 proteins physically interact with Rps21 proteins, and decreased expression of both proteins in Drosophila impairs control of cellular proliferation in hematopoietic organs during larval development. Here, we characterize the yeast RPS21A/B genes and show that strains where both genes are disrupted are not viable. Relative to the wild type, cells with disrupted RPS21A or RPS21B genes exhibit a reduction in growth rate, a decrease in free 40S subunits, an increase in the amount of free 60S subunits, and a decrease in polysome size. Ribosomal RNA processing studies reveal RPS21 and RPS0 mutants have virtually identical processing defects. The pattern of processing defects observed in RPS0 and RPS21 mutants is not a general characteristic of strains with suboptimal levels of small subunit ribosomal proteins, since disruption of the RPS18A or RPS18B genes results in related but distinct processing defects. Together, these data link the Rps0 and Rps21 proteins together functionally in promoting maturation of the 3' end of 18S rRNA and formation of active 40S ribosomal subunits.


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