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J Biol Chem, Vol. 273, Issue 21, 13104-13109, May 22, 1998

Cloning and Characterization of 4EHP, a Novel Mammalian eIF4E-related Cap-binding Protein

Eran Rom, Hyung Chan Kim, Anne-Claude Gingras, Joseph Marcotrigianod, Daniel Favre, Henrik Olseng, Stephen K. Burleydh, and Nahum Sonenberg

From the Department of Biochemistry, McGill University, Montreal, Quebec, Canada H3G1Y6, the d Laboratories of Molecular Biophysics, The Rockefeller University, New York, New York 10021, and the h Howard Hughes Medical Institute and g Human Genome Science Inc., Rockville, Maryland 25850

All eukaryotic mRNAs (except organellar) are capped at their 5' end. The cap structure (m7GpppN, where N is any nucleotide) is extremely important for the processing and translation of mRNA. Several cap-binding proteins that facilitate these processes have been characterized. Here we describe a novel human cytoplasmic protein that is 30% identical and 60% similar to the human translation initiation factor 4E (eIF4E). We demonstrate that this protein, named 4E Homologous Protein (4EHP), binds specifically to capped RNA in an ATP- and divalent ion-independent manner. The three-dimensional structure of 4EHP, as predicted by homology modeling, closely resembles that of eIF4E and site-directed mutagenesis analysis of 4EHP strongly suggests that it shares with eIF4E a common mechanism for cap binding. A putative function for 4EHP is discussed.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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