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Vol. 13, Issue 5, 1626-1640, May 2002



and
*Cell Cycle Laboratory, Medical Research Council, Radiation and
Genome Stability Unit, Harwell, Didcot, OX11 0RD, United Kingdom;
Eukaryotic translation initiation factor 3 (eIF3) is a multisubunit
complex that 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,
whereas 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 after
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 centers during environmental
stress. After heat shock, 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.
MRC Human Genetics Unit, Western General Hospital, Crewe
Road, Edinburgh, EH4 2XU, United Kingdom; and
Imperial
Cancer Research Fund, Institute of Molecular Medicine, John Radcliffe
Hospital, Oxford, OX3 9DS, United Kingdom
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