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J Biol Chem, Vol. 274, Issue 8, 4545-4550, February 19, 1999
From the In mammalian cells valyl-tRNA synthetase (ValRS)
forms a high Mr complex with the four subunits
of elongation factor EF-1H. The
Functional Interaction of Mammalian Valyl-tRNA Synthetase
with Elongation Factor EF-1
in the Complex with EF-1H
§,§,,
Laboratoire d'Enzymologie et Biochimie
Structurales, CNRS, 91190 Gif-sur-Yvette, France and the
§ Institute of Molecular Biology and Genetics, National
Academy of Sciences of Ukraine, Kiev 232143, Ukraine
, 
, and 
subunits, that
contribute the guanine nucleotide exchange activity of EF-1H, are
tightly associated with the NH2-terminal polypeptide
extension of valyl-tRNA synthetase. In this study, we have examined the
possibility that the functioning of the companion enzyme EF-1
could
regulate valyl-tRNA synthetase activity. We show here that the addition
of EF-1 and GTP in excess in the aminoacylation mixture is
accompanied by a 2-fold stimulation of valyl-tRNAVal
synthesis catalyzed by the valyl-tRNA synthetase component of the
ValRS·EF-1H complex. This effect is not observed in the presence of
EF-1 and GDP or EF-Tu·GTP and requires association of valyl-tRNA synthetase within the ValRS·EF-1H complex. Since valyl-tRNA
synthetase and elongation factor EF-1 catalyze two consecutive steps
of the in vivo tRNA cycle, aminoacylation and formation of
the ternary complex EF-1·GTP·Val-tRNAVal that serves
as a vector of tRNA from the synthetase to the ribosome, the data
suggest a coordinate regulation of these two successive reactions. The
EF-1·GTP-dependent stimulation of valyl-tRNA
synthetase activity provides further evidence for tRNA channeling
during protein synthesis in mammalian cells.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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