TY - JOUR
T1 - Cloning and characterization of 4EHP, a novel mammalian eIF4E-related cap-binding protein
AU - Rom, Eran
AU - Kim, Hyung Chan
AU - Gingras, Anne Claude
AU - Marcotrigiano, Joseph
AU - Favre, Daniel
AU - Olsen, Henrik
AU - Burley, Stephen K.
AU - Sonenberg, Nahum
PY - 1998/5/22
Y1 - 1998/5/22
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=14444274091&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=14444274091&partnerID=8YFLogxK
U2 - 10.1074/jbc.273.21.13104
DO - 10.1074/jbc.273.21.13104
M3 - Article
C2 - 9582349
AN - SCOPUS:14444274091
VL - 273
SP - 13104
EP - 13109
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 21
ER -