Krokowski D, et al. (2007) Elevated copy number of L-A virus in yeast mutant strains defective in ribosomal stalk. Biochem Biophys Res Commun 355(2):575-80
Abstract: 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.
|Status: Published||Type: Journal Article||PubMed ID: 17307145|
Topics addressed in this paper
Number of different genes curated to this paper: 13
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|Topics||Genes (#1 - 10 )|
|Protein Physical Properties|