The joining of ribosomal subunits in eukaryotes requires eIF5B

Tatyana V. Pestova (), Ivan B. Lomakin, Joon H. Lee, Sang Ki Choi, Thomas E. Dever and Christopher U. T. Hellen
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Tatyana V. Pestova: Department of Microbiology and Immunology State University of New York Health Science Center at Brooklyn
Ivan B. Lomakin: Department of Microbiology and Immunology State University of New York Health Science Center at Brooklyn
Joon H. Lee: Laboratory of Eukaryotic Gene Regulation, National Institute of Child Health and Human Development, National Institutes of Health
Sang Ki Choi: Laboratory of Eukaryotic Gene Regulation, National Institute of Child Health and Human Development, National Institutes of Health
Thomas E. Dever: Laboratory of Eukaryotic Gene Regulation, National Institute of Child Health and Human Development, National Institutes of Health
Christopher U. T. Hellen: Department of Microbiology and Immunology State University of New York Health Science Center at Brooklyn

Nature, 2000, vol. 403, issue 6767, 332-335

Abstract: Abstract Initiation of eukaryotic protein synthesis begins with the ribosome separated into its 40S and 60S subunits1. The 40S subunit first binds eukaryotic initiation factor (eIF) 3 and an eIF2–GTP–initiator transfer RNA ternary complex. The resulting complex requires eIF1, eIF1A, eIF4A, eIF4B and eIF4F to bind to a messenger RNA and to scan to the initiation codon2. eIF5 stimulates hydrolysis of eIF2-bound GTP and eIF2 is released from the 48S complex formed at the initiation codon before it is joined by a 60S subunit to form an active 80S ribosome3,4,5,6,7,8. Here we show that hydrolysis of eIF2-bound GTP induced by eIF5 in 48S complexes is necessary but not sufficient for the subunits to join. A second factor termed eIF5B (relative molecular mass 175,000) is essential for this process. It is a homologue of the prokaryotic initiation factor IF2 (refs 6, 7) and, like it8,9,10,11,12, mediates joining of subunits and has a ribosome-dependent GTPase activity that is essential for its function.

Date: 2000
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DOI: 10.1038/35002118

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