TY - JOUR
T1 - The eIF3 Interactome Reveals the Translasome, a Supercomplex Linking Protein Synthesis and Degradation Machineries
AU - Sha, Zhe
AU - Brill, Laurence M.
AU - Cabrera, Rodrigo
AU - Kleifeld, Oded
AU - Scheliga, Judith S.
AU - Glickman, Michael H.
AU - Chang, Eric C.
AU - Wolf, Dieter A.
N1 - Funding Information:
We thank D. Balasundaram (Singapore University) for providing materials, M. Petroski for reviewing the manuscript, and K. Motamedchaboki and A. Iranli for bioinformatics support. We also thank Mike Mancini and his staff at the Integrated Microscopy Core at the Dan Duncan Cancer Center for technical assistance. This work was funded by NSF grant 0920229 and NIH grant GM059780 to D.A.W. and by NIH grants CA90464 and CA107187 to E.C.C.; Z.S. was supported by a predoctoral fellowship from the DOD (BC030443). L.M.B. is funded through the NIH Center Grants 5 P30 CA30199-28 and 5 P30 NS057096. We also thank Glen and Judy Smith for their generous support.
PY - 2009/10/9
Y1 - 2009/10/9
N2 - 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-β Kap123p and Sal3p. Our genetic data indicated that the binding to both importins-β 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.
AB - 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-β Kap123p and Sal3p. Our genetic data indicated that the binding to both importins-β 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.
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U2 - 10.1016/j.molcel.2009.09.026
DO - 10.1016/j.molcel.2009.09.026
M3 - Article
C2 - 19818717
AN - SCOPUS:70349780560
SN - 1097-2765
VL - 36
SP - 141
EP - 152
JO - Molecular Cell
JF - Molecular Cell
IS - 1
ER -