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Molecular and Cellular Biology, November 2002, p. 7853-7867, Vol. 22, No. 22
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.22.7853-7867.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The Histone 3'-Terminal Stem-Loop-Binding Protein Enhances Translation through a Functional and Physical Interaction with Eukaryotic Initiation Factor 4G (eIF4G) and eIF3

Jun Ling,1 Simon J. Morley,2 Virginia M. Pain,2 William F. Marzluff,3 and Daniel R. Gallie1*

Department of Biochemistry, University of California, Riverside, California 92521-0129,1 Biochemistry Laboratory, School of Biological Sciences, University of Sussex, Falmer, Brighton BN1 9QG, United Kingdom,2 Program in Molecular Biology and Biotechnology, University of North Carolina, Chapel Hill, North Carolina 275993

Received 12 July 2002/ Accepted 13 August 2002

Metazoan cell cycle-regulated histone mRNAs are unique cellular mRNAs in that they terminate in a highly conserved stem-loop structure instead of a poly(A) tail. Not only is the stem-loop structure necessary for 3'-end formation but it regulates the stability and translational efficiency of histone mRNAs. The histone stem-loop structure is recognized by the stem-loop-binding protein (SLBP), which is required for the regulation of mRNA processing and turnover. In this study, we show that SLBP is required for the translation of mRNAs containing the histone stem-loop structure. Moreover, we show that the translation of mRNAs ending in the histone stem-loop is stimulated in Saccharomyces cerevisiae cells expressing mammalian SLBP. The translational function of SLBP genetically required eukaryotic initiation factor 4E (eIF4E), eIF4G, and eIF3, and expressed SLBP coisolated with S. cerevisiae initiation factor complexes that bound the 5' cap in a manner dependent on eIF4G and eIF3. Furthermore, eIF4G coimmunoprecipitated with endogenous SLBP in mammalian cell extracts and recombinant SLBP and eIF4G coisolated. These data indicate that SLBP stimulates the translation of histone mRNAs through a functional interaction with both the mRNA stem-loop and the 5' cap that is mediated by eIF4G and eIF3.

* Corresponding author. Mailing address: Department of Biochemistry, University of California, Riverside, CA 92521-0129. Phone: (909) 787-7298. Fax: (909) 787-3590. E-mail: drgallie{at}citrus.ucr.edu.

Molecular and Cellular Biology, November 2002, p. 7853-7867, Vol. 22, No. 22
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.22.7853-7867.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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