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Cloning and characterization of the gene encoding ribosomal P0 phosphoprotein from Neurospora crassa.

100%
Krokowski D., Tchórzewski M., Grankowski N.
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2002
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vol. 49
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issue 1
11-18
EN
A gene for ribosomal protein P0 that belongs to the family of ribosomal P proteins was isolated from a Neurospora crassa cDNA library, using polyclonal antibodies against recombinant P0 protein from Saccharomyces cerevisiae. This is the first gene for ribosomal P0 protein to be cloned from filamentous fungi. The derived P0 protein sequence has a strong homology to other eukaryotic P0 proteins; yet, there is a notable alteration in the conservative C-terminal region, placing this protein among the unique sequences from protozoan parasites.
2
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Extraribosomal function of the acidic ribosomal P1-protein YP1α from Saccharomyces cerevisiae

100%
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.
3
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The 45 kDa and 27 kDa yeast's protein kinases are not immunologically related

88%
Szyszka R., Tchórzewski M., Dukowski P., Winiarczyk S., Gąiasior E.
Acta Biochimica Polonica
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1992
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vol. 39
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issue 2
205-213
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