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Molecular and Cellular Biology, October 2000, p. 7183-7191, Vol. 20, No. 19
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Physical and Functional Interaction between the Eukaryotic Orthologs of Prokaryotic Translation Initiation Factors IF1 and IF2

Sang Ki Choi,1 DeAnne S. Olsen,1 Antonina Roll-Mecak,2 Agnes Martung,1 Keith L. Remo,1 Stephen K. Burley,2,3 Alan G. Hinnebusch,1 and Thomas E. Dever1,*

Laboratory of Eukaryotic Gene Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892,1 and Laboratories of Molecular Biophysics2 and Howard Hughes Medical Institute,3 The Rockefeller University, New York, New York 10021

Received 28 March 2000/Returned for modification 25 May 2000/Accepted 13 July 2000

To initiate protein synthesis, a ribosome with bound initiator methionyl-tRNA must be assembled at the start codon of an mRNA. This process requires the coordinated activities of three translation initiation factors (IF) in prokaryotes and at least 12 translation initiation factors in eukaryotes (eIF). The factors eIF1A and eIF5B from eukaryotes show extensive amino acid sequence similarity to the factors IF1 and IF2 from prokaryotes. By a combination of two-hybrid, coimmunoprecipitation, and in vitro binding assays eIF1A and eIF5B were found to interact directly, and the eIF1A binding site was mapped to the C-terminal region of eIF5B. This portion of eIF5B was found to be critical for growth in vivo and for translation in vitro. Overexpression of eIF1A exacerbated the slow-growth phenotype of yeast strains expressing C-terminally truncated eIF5B. These findings indicate that the physical interaction between the evolutionarily conserved factors eIF1A and eIF5B plays an important role in translation initiation, perhaps to direct or stabilize the binding of methionyl-tRNA to the ribosomal P site.

* Corresponding author. Mailing address: National Institutes of Health, 6 Center Dr., Bldg. 6A/Rm. B1A-02, Bethesda, MD 20892-2716. Phone: (301) 496-4519. Fax: (301) 496-8576. E-mail: tdever{at}box-t.nih.gov.

Molecular and Cellular Biology, October 2000, p. 7183-7191, Vol. 20, No. 19
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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