Journal
MOLECULAR CELL
Volume 36, Issue 1, Pages 141-152Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2009.09.026
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Funding
- NSF [0920229]
- NIH [GM059780, CA90464, CA107187, 5 P30 CA30199-28, 5 P30NS057096]
- DOD [BC030443]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0920229] Funding Source: National Science Foundation
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elF3 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 elF3 interactome, which was found to contain 230 proteins. elF3 assembles into a large supercomplex, the translasome, which contains elongation factors, tRNA synthetases, 40S and 60S ribosomal proteins, chaperones, and the proteasome. elF3 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 elF3 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.
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