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Volume 272, Number 52, Issue of December 26, 1997 pp. 33290-33297

Recombinant Subunits of Mammalian Elongation Factor 1 Expressed in Escherichia coli
SUBUNIT INTERACTIONS, ELONGATION ACTIVITY, AND PHOSPHORYLATION BY PROTEIN KINASE CKII

(Received for publication, May 21, 1997, and in revised form, September 10, 1997)

From the Department of Biochemistry and the Genetics Graduate Group, University of California, Riverside, California 92521-0129

The first step in elongation requires two different activities; elongation factor (EF)-1 transfers aminoacyl-tRNA to the ribosome and is released upon hydrolysis of GTP, EF-1 catalyzes exchange of GDP on EF-1 with GTP. To analyze the role of the individual subunits of EF-1 in elongation, the cDNAs for the , , and  subunits of EF-1 from rabbit were cloned, and proteins of 225, 437, and 280 amino acids, respectively, were expressed in Escherichia coli. The purified recombinant  subunit migrates as a dimer and the  subunit as a trimer upon gel filtration, whereas the  subunit forms a large aggregate. Complexes of , and were formed by self-association and eluted with a molecular mass of approximately 160, 530, and 670 kDa, respectively; no interaction was observed between  and . The activity of the recombinant subunits was determined with native EF-1 by measuring stimulation of the rate of elongation by poly(U)-directed polyphenylalanine synthesis. Recombinant  and  alone stimulated the rate of elongation by 10-fold, with a ratio of 5:2 or . The complex stimulated EF-1 activity up to 10-fold with a ratio of 20 to 1. Phosphorylation of the  and  subunits alone or in by protein kinase CKII had no effect on the rate of elongation.

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