The RPS26A and RPS26B isogenes of Saccharomyces cerevisiae encode two almost identical proteins of the small 40S ribosomal subunit, which differ by only two amino acid residues. Growth of an rps26BΔ mutant strain is normal, whereas an rps26AΔ strain displays a reduced growth rate and increased sensitivity towards the specific translational inhibitor paromomycin. An rps26AΔ rps26BΔ double mutant strain is inviable. RPS26A but not RPS26B is required for haploid adhesive and diploid pseudohyphal growth mediated by FLO11, which encodes an adhesion. The RPS26A and RPS26B transcripts make up about 70 and 30% of the cellular RPS26 mRNA, respectively. Overexpression of RPS26B, as well as an RPS26B open reading frame driven by the RPS26A promoter, complements the rps26AΔ deletion and restores haploid invasive growth as well as diploid pseudohyphal growth. These results suggest that the two proteins are functionally interchangeable. FLO11-lacZ activity is not present in haploid rps26AΔ yeast mutant strains, even though FLO11 mRNA levels are not reduced. This suggests that the amount of Rps26p is critical for accurate translation of the FLO11 mRNA, and therefore for the dimorphic switch of the baker's yeast from a single cell yeast to an adhesive filamentous growth form.