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

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 v...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2007-04, Vol.355 (2), p.575-580
Main Authors: Krokowski, Dawid, Tchorzewski, Marek, Boguszewska, Aleksandra, Mckay, Adam R., Maslen, Sarah L., Robinson, Carol V., Grankowski, Nikodem
Format: Article
Language:English
Subjects:
Capsid Proteins - metabolism
Chromatography, Affinity
Electrophoresis, Polyacrylamide Gel
Hygromycin B - pharmacology
L-A virus
Mutation
P-protein
Paromomycin - pharmacology
Proteome
Ribosomal stalk
Ribosomes
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - virology
Tandem Mass Spectrometry
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2007.02.024