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Extraribosomal function of the acidic ribosomal P1-protein YP1alpha from Saccharomyces cerevisiae

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Tchorzewski M., Boldyreff B., Grankowski N.

Acta Biochimica Polonica

1999

tom 46

nr 4

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.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Boldyreff B.

1 Grankowski N.

1 Tchorzewski M.

1 1999

Wyniki wyszukiwania

Extraribosomal function of the acidic ribosomal P1-protein YP1alpha from Saccharomyces cerevisiae