Nelson, M.R., Luo, H., Vari, H.K., Cox, B.J., Simmonds, A.J., Krause, H.M., Lipshitz, H.D., Smibert, C.A. (2007). A multiprotein complex that mediates translational enhancement in drosophila.  J. Biol. Chem. 282(47): 34031--34038.

FBrf0202607

Research paper

Modulating the efficiency of translation plays an important role in a wide variety of cellular processes and is often mediated by trans-acting factors that interact with cis-acting sequences within the mRNA. Here we show that a cis-acting element, the Hsp83 degradation element (HDE), within the 3'-untranslated region of the Drosophila Hsp83 mRNA functions as a translational enhancer. We show that this element is bound by a multiprotein complex, and we identify components using a novel affinity-based method called tandem RNA affinity purification tagging. Three proteins (DDP1, Hrp48, and poly(A)-binding protein) are components of the HDE-binding complex and function in translational enhancement. Our data support a model whereby the HDE is composed of several cis-acting subelements that represent binding sites for trans-acting factors, and the combined action of these trans-acting factors underlies the ability of the HDE to stimulate translation.