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Background  In plants, each ribosomal protein (RP) is encoded by a small gene family but it is largely unknown whether the family members are functionally diversified. There are two  RPL23a  paralogous genes ( RPL23aA  and  RPL23aB ) encoding cytoplasmic ribosomal proteins in  Arabidopsis thaliana . Knock-down of  RPL23aA  using RNAi impeded growth and led to morphological abnormalities, whereas knock-out of  RPL23aB  had no observable phenotype, thus these two RPL23a paralogous proteins have been used as examples of ribosomal protein paralogues with functional divergence in many published papers.    Results  In this study, we characterized T-DNA insertion mutants of  RPL23aA  and  RPL23aB . A rare non-allelic non-complementation phenomenon was found in the F1 progeny of the  rpl23aa  X  rpl23ab  cross, which revealed a dosage effect of these two genes. Both  RPL23aA  and  RPL23aB  were found to be expressed almost in all examined tissues as revealed by GUS reporter analysis. Expression of  RPL23aB  driven by the  RPL23aA  promoter can rescue the phenotype of  rpl23aa , indicating these two proteins are actually equivalent in function. Interestingly, based on the publicly available RNA-seq data, we found that these two  RPL23a  paralogues were expressed in a concerted manner and the expression level of  RPL23aA  was much higher than that of  RPL23aB  at different developmental stages and in different tissues.    Conclusions  Our findings suggest that the two RPL23a paralogous proteins are functionally equivalent but the two genes are not.  RPL23aA  plays a predominant role due to its higher expression levels.  RPL23aB  plays a lesser role due to its lower expression. The presence of paralogous genes for the RPL23a protein in plants might be necessary to maintain its adequate dosage.

Arabidopsis paralogous genes RPL23aA and RPL23aB encode functionally equivalent proteins