کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1937461 | 1050716 | 2007 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Elevated copy number of L-A virus in yeast mutant strains defective in ribosomal stalk Elevated copy number of L-A virus in yeast mutant strains defective in ribosomal stalk](/preview/png/1937461.png)
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.
Journal: Biochemical and Biophysical Research Communications - Volume 355, Issue 2, 6 April 2007, Pages 575–580