Cloning and characterization of 4EHP, a novel mammalian eIF4E-related cap-binding protein

Eran Rom, Hyung Chan Kim, Anne Claude Gingras, Joseph Marcotrigiano, Daniel Favre, Henrik Olsen, Stephen K. Burley, Nahum Sonenberg

Research output: Contribution to journalArticle

94 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)13104-13109
Number of pages6
JournalJournal of Biological Chemistry
Volume273
Issue number21
DOIs
StatePublished - May 22 1998
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Rom, E., Kim, H. C., Gingras, A. C., Marcotrigiano, J., Favre, D., Olsen, H., Burley, S. K., & Sonenberg, N. (1998). Cloning and characterization of 4EHP, a novel mammalian eIF4E-related cap-binding protein. Journal of Biological Chemistry, 273(21), 13104-13109. https://doi.org/10.1074/jbc.273.21.13104