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 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.
Krokowski
Dawid
D
Department of Molecular Biology, Maria Curie-Skłodowska University, Akademicka 19, 20-033 Lublin, Poland.
Tchorzewski
Marek
M
Boguszewska
Aleksandra
A
McKay
Adam R
AR
Maslen
Sarah L
SL
Robinson
Carol V
CV
Grankowski
Nikodem
N
D036022:Capsid Proteins / Q000378:metabolism; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006921:Hygromycin B / Q000494:pharmacology; D009154:Mutation; D010303:Paromomycin / Q000494:pharmacology; D020543:Proteome; D012270:Ribosomes; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000821:virology*; D053719:Tandem Mass Spectrometry
D036022:Capsid Proteins; D020543:Proteome; D006921:Hygromycin B; D010303:Paromomycin