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

• Authors: Marek Tchórzewski , Brigitte Boldyreff , Nikodem Grankowski
• Languages of publication: EN

Abstracts

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.

Keywords

EN

acidic ribosomal P-protein; transactivation; translation; yeast

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 1999
• Volume: 46
• Issue: 4
• Pages: 901-910

Dates

published

1999

received

1999-07-05

accepted

1999-11-04

Contributors

author

Marek Tchórzewski

• Maria Curie-Skłodowska University, Institute of Microbiology and Biotechnology, Department of Molecular Biology, Akademicka 19, 20-033 Lublin, Poland

author

Brigitte Boldyreff

• Odense University, Institute of Biochemistry, Campusvej 55, DK-5230 Odense, Denmark

author

Nikodem Grankowski

• Maria Curie-Skłodowska University, Institute of Microbiology and Biotechnology, Department of Molecular Biology, Akademicka 19, 20-033 Lublin, Poland