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A more recent version of this article appeared on May 1, 2002
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Submitted on June 20, 2001
Revised on December 27, 2001
Accepted on February 4, 2002
1 MRC Radiation and Genome Stability Unit, Harwell, Didcot, OX11 0RD, U.K.
2 MRC Human Genetics Unit, Western General Hospital, Crewe Road, Edinburgh, EH4 2XU, U.K.
3 Imperial Cancer Research Fund, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, OX3 9DS, U.K.
* Corresponding author. E-mail address: T.Humphrey{at}har.mrc.ac.uk.
Eukaryotic translation initiation factor 3 (eIF3) is a multisubunit complex which plays a central role in translation initiation. We show that fission yeast Sum1, which is structurally related to known eIF3 subunits in other species, is essential for translation initiation, while its overexpression results in reduced global translation. Sum1 is associated with the 40S ribosome, and interacts stably with Int6, an eIF3 component, in vivo, suggesting that Sum1 is a component of the eIF3 complex. Sum1 is cytoplasmic under normal growth conditions. Surprisingly, Sum1 is rapidly relocalized to cytoplasmic foci following osmotic and thermal stress. Int6 and p116, another putative eIF3 subunit, behave similarly, suggesting that eIF3 is a dynamic complex. These cytoplasmic foci, which additionally comprise eIF4E and RNA components, may function as translation centres during environmental stress. Following heatshock, Sum1 additionally colocalizes stably with the 26S proteasome at the nuclear periphery. The relationship between Sum1 and the 26S proteasome was further investigated, and we find cytoplasmic Sum1 localization to be dependent on the 26S proteasome. Furthermore, Sum1 interacts with the Mts2 and Mts4 components of the 26S proteasome. These data indicate a functional link between components of the structurally related eIF3 translation initiation and 26S proteasome complexes.
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