The stem-loop binding protein stimulates histone translation at an early step in the initiation pathway

Gorgoni, Barbara; Andrews, Stuart; Schaller, André; Schümperli, Daniel; Gray, Nicola K; Müller, Berndt (2005). The stem-loop binding protein stimulates histone translation at an early step in the initiation pathway. RNA - a publication of the RNA Society, 11(7), pp. 1030-1042. Woodbury, N.Y.: Cold Spring Harbor Laboratory Press 10.1261/rna.7281305

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Metazoan replication-dependent histone mRNAs do not have a poly(A) tail but end instead in a conserved stem-loop structure. Efficient translation of these mRNAs is dependent on the stem-loop binding protein (SLBP). Here we explore the mechanism by which SLBP stimulates translation in vertebrate cells, using the tethered function assay and analyzing protein-protein interactions. We show for the first time that translational stimulation by SLBP increases during oocyte maturation and that SLBP stimulates translation at the level of initiation. We demonstrate that SLBP can interact directly with subunit h of eIF3 and with Paip1; however, neither of these interactions is sufficient to mediate its effects on translation. We find that Xenopus SLBP1 functions primarily at an early stage in the cap-dependent initiation pathway, targeting small ribosomal subunit recruitment. Analysis of IRES-driven translation in Xenopus oocytes suggests that SLBP activity requires eIF4E. We propose a model in which a novel factor contacts eIF4E bound to the 5' cap and SLBP bound to the 3' end simultaneously, mediating formation of an alternative end-to-end complex.

Item Type:

Journal Article (Original Article)


08 Faculty of Science > Department of Biology > Institute of Cell Biology
04 Faculty of Medicine > Department of Gynaecology, Paediatrics and Endocrinology (DFKE) > Clinic of Paediatric Medicine

UniBE Contributor:

Schaller, André, Schümperli, Daniel


500 Science > 570 Life sciences; biology




Cold Spring Harbor Laboratory Press




Anette van Dorland

Date Deposited:

04 Oct 2013 15:13

Last Modified:

05 Dec 2022 14:22

Publisher DOI:


PubMed ID:


Web of Science ID:


URI: (FactScience: 197377)

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