The eIF3 interactome reveals the translasome, a supercomplex linking protein synthesis and degradation machineries

Zhe Sha, Laurence M Brill, Rodrigo Cabrera, Oded Kleifeld, Judith S Scheliga, Michael H Glickman, Eric C Chang, Dieter A Wolf

Research output: Contribution to journalArticleResearchpeer-review

95 Citations (Scopus)

Abstract

eIF3 promotes translation initiation, but relatively little is known about its full range of activities in the cell. Here, we employed affinity purification and highly sensitive LC-MS/MS to decipher the fission yeast eIF3 interactome, which was found to contain 230 proteins. eIF3 assembles into a large supercomplex, the translasome, which contains elongation factors, tRNA synthetases, 40S and 60S ribosomal proteins, chaperones, and the proteasome. eIF3 also associates with ribosome biogenesis factors and the importins-beta Kap123p and Sal3p. Our genetic data indicated that the binding to both importins-beta is essential for cell growth, and photobleaching experiments revealed a critical role for Sal3p in the nuclear import of one of the translasome constituents, the proteasome. Our data reveal the breadth of the eIF3 interactome and suggest that factors involved in translation initiation, ribosome biogenesis, translation elongation, quality control, and transport are physically linked to facilitate efficient protein synthesis.
Original languageEnglish
Pages (from-to)141 - 152
Number of pages12
JournalMolecular Cell
Volume36
Issue number1
DOIs
Publication statusPublished - 2009
Externally publishedYes

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