ArticleProtein science : a publication of the Protein Society2014
Only a subset of the PAB1-mRNP proteome is present in mRNA translation complexes.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- The response to single-gene duplication implicates translation as a key vulnerability in aneuploid yeast.PLoS genetics · 2024Article
- Post-transcriptional control of fungal cell wall synthesis.Cell surface (Amsterdam, Netherlands) · 2022Article
- Article
- The GUL-1 Protein Binds Multiple RNAs Involved in Cell Wall Remodeling and Affects the MAK-1 Pathway inFrontiers in fungal biology · 2021Article
- Identification of a 57S translation complex containing closed-loop factors and the 60S ribosome subunit.Scientific reports · 2018Article
- Article
- Sbp1 modulates the translation of Pab1 mRNA in a poly(A)- and RGG-dependent manner.RNA (New York, N.Y.) · 2018Article
- Phosphorylation and nuclear transit modulate the balance between normal function and terminal aggregation of the yeast RNA-binding protein Ssd1.Molecular biology of the cell · 2017Article
- The La and related RNA-binding proteins (LARPs): structures, functions, and evolving perspectives.Wiley interdisciplinary reviews. RNA · 2017Review
- The Aspergillus nidulans Pbp1 homolog is required for normal sexual development and secondary metabolism.Fungal genetics and biology : FG & B · 2017Article
- Multiple discrete soluble aggregates influence polyglutamine toxicity in a Huntington's disease model system.Scientific reports · 2016Article
- Stoichiometry and Change of the mRNA Closed-Loop Factors as Translating Ribosomes Transit from Initiation to Elongation.PloS one · 2016Article
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7 authors at 1 institution in 1 country.
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Abstract
We have previously identified 55 nonribosomal proteins in PAB1-mRNP complexes in Saccharomyces cerevisiae using mass spectrometric analysis. Because one of the inherent limitations of mass spectrometry is that it does not inform as to the size or type of complexes in which the proteins are present, we consequently used analytical ultracentrifugation with fluorescent detection system (AU-FDS) to determine which proteins are present in the 77S monosomal translation complex that contains minimally the closed-loop structure components (eIF4E, eIF4G, and PAB1), mRNA, and the 40S and 60S ribosomes. We assayed by AU-FDS analysis 33 additional PAB1-mRNP factors but found that only five of these proteins were present in the 77S translation complex: eRF1, SLF1, SSD1, PUB1, and SBP1. eRF1 is involved in translation termination, SBP1 is a translational repressor, and SLF1, SSD1, and PUB1 are known mRNA binding proteins. Many of the known P body/stress granule proteins that associate with the PAB1-mRNP were not present in the 77S translation complex, implying that P body/stress granules result from significant protein additions after translational cessation. These data inform that AU-FDS can clarify protein complex identification that remains undetermined after typical immunoprecipitation and mass spectrometric analyses.
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