Nucleic Acids Research, Vol 27, Issue 5 1331-1337, Copyright © 1999 by Oxford University Press
A Bandyopadhyay and U Maitra
Eukaryotic translation initiation factor 3 (eIF3) is a large multisubunit
protein complex that plays an essential role in the binding of the
initiator methionyl-tRNA and mRNA to the 40S ribosomal subunit to form the
40S initiation complex. cDNAs encoding all the subunits of mammalian eIF3
except the p42 subunit have been cloned in several laboratories. Here we
report the cloning and characterization of a human cDNA encoding the p42
subunit of mammalian eIF3. The open reading frame of the cDNA, which
encodes a protein of 320 amino acids (calculated Mr35 614) has been
expressed in Escherichia coli and the recombinant protein has been purified
to homogeneity. The purified protein binds RNA in agreement with the
presence of a putative RNA binding motif in the deduced amino acid
sequence. The protein shows 33% identity and 53% similarity with the Tif35p
subunit (YDR 429C) of yeast eIF3. Transfection experiments demonstrated
that polyhistidine-tagged p42 protein, transiently expressed in human U20S
cells, was incorporated into endogenous eIF3. Furthermore, eIF3 isolated
from transfected cell lysates contains bound eIF5 indicating that a
specific physical interaction between eIF5 and eIF3 may play an important
role in the function of eIF5 during translation initiation in eukaryotic
cells.
ARTICLES
Cloning and characterization of the p42 subunit of mammalian translation initiation factor 3 (eIF3): demonstration that eIF3 interacts with eIF5 in mammalian cells
Department of Developmental and Molecular Biology, Albert Einstein College of Medicine of Yeshiva University,Jack and Pearl Resnick Campus, Bronx, New York, NY 10461, USA.
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