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Extraribosomal function of the acidic ribosomal P1-protein YP1α from Saccharomyces cerevisiae

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Tchórzewski M., Boldyreff B., Grankowski N.
Acta Biochimica Polonica
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1999
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vol. 46
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issue 4
901-910
EN
The yeast acidic ribosomal P-proteins YP1α, YP1β, YP2a and YP2b were studied for a possible transactivation potential beside their ribosomal function. The fusions of P-proteins with the GAL4 DNA-binding domain were assayed toward their transcriptional activity with the aid of reporter genes in yeast. Two of the P-proteins, YP1α and YP1β, exhibited transactivation potential, however, only YP1α can be regarded as a potent transactivator. This protein was able to transactivate a reporter gene associated with two distinct promoter systems, GAL1 or CYC1. Additionally, truncated proteins of YP1α and YP1β were analyzed. The N-terminal part of YP1α fused to GAL4-BD showed transactivation potential but the C-terminal part did not. Our results suggest a putative extraribosomal function for these ribosomal proteins which consequently may be classified as "moonlighting" proteins.
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