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

Authors :
Brigitte Boldyreff
Marek Tchórzewski
Nikodem Grankowski
Source :
Acta biochimica Polonica. 46(4)
Publication Year :
2000

Abstract

The yeast acidic ribosomal P-proteins YP1alpha, YP1beta, YP2alpha and YP2beta 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, YP1alpha and YP1beta, exhibited transactivation potential, however, only YP1alpha 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 YP1alpha and YP1beta were analyzed. The N-terminal part of YP1alpha 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.

Details

ISSN :
0001527X
Volume :
46
Issue :
4
Database :
OpenAIRE
Journal :
Acta biochimica Polonica
Accession number :
edsair.doi.dedup.....bfcc3dcf2d29fe633ee2458a8a63bd63