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Biochem Biophys Res Commun. 2007 Apr 6;355(2):575-80. Epub 2007 Feb 12.

Elevated copy number of L-A virus in yeast mutant strains defective in ribosomal stalk.

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  • 1Department of Molecular Biology, Maria Curie-SkÅ‚odowska University, Akademicka 19, 20-033 Lublin, Poland.


The eukaryotic ribosomal stalk, composed of the P-proteins, is a part of the GTPase-associated-center which is directly responsible for stimulation of translation-factor-dependent GTP hydrolysis. Here we report that yeast mutant strains lacking P1/P2-proteins show high propagation of the yeast L-A virus. Affinity-capture-MS analysis of a protein complex isolated from a yeast mutant strain lacking the P1A/P2B proteins using anti-P0 antibodies showed that the Gag protein, the major coat protein of the L-A capsid, is associated with the ribosomal stalk. Proteomic analysis revealed that the elongation factor eEF1A was also present in the isolated complex. Additionally, yeast strains lacking the P1/P2-proteins are hypersensitive to paromomycin and hygromycin B, underscoring the fact that structural perturbations in the stalk strongly influence the ribosome function, especially at the level of elongation.

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