Rat RL23a ribosomal protein efficiently competes with its Saccharomyces cerevisiae L25 homologue for assembly into 60 S subunits

Journal of Molecular Biology
R E JeeningaH A Raué

Abstract

The large subunit protein RL23a from rat liver ribosomes shows 62% sequence identity with the primary rRNA-binding ribosomal protein L25 from Saccharomyces cerevisiae. In vitro binding studies indicated that both r-proteins are able to recognise the L25 binding site on yeast 25 S rRNA and its structural homologue on mammalian 28 S rRNA with equal efficiency. To determine whether the two r-proteins are also functionally equivalent in vivo, a single plasmid-borne copy of either the wild-type L25 gene or the RL23a cDNA, driven by the L25 promoter, was introduced into a yeast strain in which the chromosomal L25 gene is under control of the glucose-repressible GALI-10 promoter. No difference in growth rate could be detected between the two types of transformants when cultured on glucose-based medium. In cells that co-express epitope-tagged versions of L25 and RL23a from single-copy genes, approximately 35% of the 60 S subunits contained the heterologous protein as determined by Western analysis. This value could be increased to 55% by overexpressing RL23a using a multi-copy plasmid. These data demonstrate that rat RL23a can act as a highly efficient substitute for its yeast counterpart in the assembly of functional yeast ribosomes e...Continue Reading

Citations

Jun 16, 2005·Plant Physiology·María Eugenia ZanettiJulia Bailey-Serres
Jan 26, 2002·Molecular and Cellular Biology·Scott M Plafker, Ian G Macara
Aug 27, 2005·Genome Génome / Conseil National De Recherches Canada·Kerri B McIntosh, Peta C Bonham-Smith

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